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2',3'-cyclic RNAn + phosphate
RNA(n-1) + a nucleotide diphosphate
-
-
-
?
24-nucleotide RNA molecule + ADP
25-nucleotide RNA molecule + phosphate
-
when both ADP and phosphate are present at the reaction mixture, the direction of activity, either polyadenylation or degradation, is dependent on their relative concentrations
-
-
r
24-nucleotide RNA molecule + phosphate
23-nucleotide RNA molecule + nucleoside diphosphate
-
when both ADP and phosphate are present at the reaction mixture, the direction of activity, either polyadenylation or degradation, is dependent on their relative concentrations
-
-
r
3'-phosphorylated RNA(n) + phosphate
RNA(n-1) + a nucleotide diphosphate
-
enzyme inefficiently degrades 3'-phosphorylated RNA
-
?
ADP + globin mRNAn
globin mRNAn+1 + phosphate
-
-
-
-
?
microR-221 RNAn+1 + phosphate
microR-221 RNAn + ADP
-
recombinantly expressed microRNAs miR-let7a, miR-106b, miR-25, miR-221, miR-222, and miR-184 as substrates, the recombinant enzyme selectively and preferentially degrades microRNA-221 in human melanoma cells
-
-
r
microRNAn+1 + phosphate
microRNAn + ADP
-
recombinantly expressed microRNAs miR-let7a, miR-106b, miR-25, miR-221, miR-222, and miR-184
-
-
r
pJFD4 HpaI RNA+1 + phosphate
pJFD4 HpaI RNA + nucleoside diphosphate
-
derivative of SP82 phage RNA, arsenate can replace phosphate
-
?
poly(A) + ADP
poly(A)+1 + phosphate
poly(A)(n-1) + ADP
poly(A)n + phosphate
poly(A)+1 + phosphate
poly(A) + ADP
poly(A)n + phosphate
poly(A)(n-1) + ADP
poly(C) + CDP
poly(C)+1 + phosphate
poly(C)+1 + phosphate
poly(C) + ADP
poly(G) + GDP
poly(G)+1 + phosphate
poly(I) + IDP
poly(I)+1 + phosphate
poly(U)+ UDP
poly(U)+1 + phosphate
poly(U)+1 + phosphate
poly(U) + ADP
polyadenylic acid + phosphate
? + ADP
-
-
-
-
?
polycytidylic acid + phosphate
? + CDP
-
-
-
-
?
polyguanylic acid + phosphate
? + GDP
-
-
-
-
?
polyuridylic acid + phosphate
? + UDP
-
-
-
-
?
rabbit globin mRNAn+1 + phosphate
ADP + rabbit globin mRNAn
-
only the poly(A) tail of the mRNA is removed
-
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
RNA + ATP
RNA+1 + diphosphate
-
polymerization in the absence of phosphate
-
r
RNA + CTP
RNA+1 + diphosphate
-
polymerization in the absence of phosphate
-
r
RNA + GTP
RNA+1 + diphosphate
-
polymerization in the absence of phosphate
-
r
RNA + UTP
RNA+1 + diphosphate
-
polymerization in the absence of phosphate
-
r
RNA(n) + phosphate
RNA(n-1) + a nucleotide diphosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
RNAn + UDP
RNAn+1 + phosphate
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
yeast RNA+1 + phosphate
yeast RNA + nucleoside diphosphate
-
2% of activity with poly(U)
-
?
additional information
?
-
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
no phosphorolysis activity with poly(G)
?
poly(A) + ADP
poly(A)+1 + phosphate
-
-
no phosphorolysis activity with poly(G)
?
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
?
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
strong preference for ADP and poly(A) in phosphorolysis and polymerization reaction
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
-
?
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
poly(A) polymerization product containing 8000-13000 nucleotides
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
32% of activity with poly(U) in phosphorolysis reaction
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
chloroplast PNPase has both exonuclease and poly(A) polymerase activity, phosphate enhances RNA degradation activity, ADP inhibits degradation and enhances poly(A) polymerization, ADP best substrate
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
-
-
r
poly(A) + ADP
poly(A)+1 + phosphate
-
primer required for polymerization
-
r
poly(A)(n-1) + ADP
poly(A)n + phosphate
-
-
-
r
poly(A)(n-1) + ADP
poly(A)n + phosphate
-
-
-
r
poly(A)(n-1) + ADP
poly(A)n + phosphate
-
-
-
r
poly(A)+1 + phosphate
poly(A) + ADP
-
-
-
r
poly(A)+1 + phosphate
poly(A) + ADP
-
-
-
r
poly(A)+1 + phosphate
poly(A) + ADP
-
-
-
ir
poly(A)+1 + phosphate
poly(A) + ADP
-
-
-
r
poly(A)n + phosphate
poly(A)(n-1) + ADP
-
-
-
r
poly(A)n + phosphate
poly(A)(n-1) + ADP
-
-
-
r
poly(A)n + phosphate
poly(A)(n-1) + ADP
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
51% of activity with ADP
21% of activity with poly(U) in phosphorolysis reaction
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
low poly(C) phosphorolysis activity
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
-
-
r
poly(C) + CDP
poly(C)+1 + phosphate
-
primer required for polymerization
-
r
poly(C)+1 + phosphate
poly(C) + ADP
-
-
-
ir
poly(C)+1 + phosphate
poly(C) + ADP
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
much lower activity than with ADP, activity depends on polyribonucleotide primer
-
-
?
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
very little activity
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
10% of activity with ADP and poly(A)
less than 15% of phosphorolysis activity with poly(A)
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
GDP second best substrate
-
-
?
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
-
-
r
poly(G) + GDP
poly(G)+1 + phosphate
-
primer required for polymerization
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
?
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
phosphorolysis at 14% of activity with poly(A)
?
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
48% of activity with ADP
28% of activity with poly(U) in phosphorolysis reaction
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
-
-
r
poly(I) + IDP
poly(I)+1 + phosphate
-
primer required for polymerization
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
-
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
-
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
55% of activity with ADP
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
best substrate for phosphorolysis reaction
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
-
lower activity than with poly(A)
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
-
-
r
poly(U)+ UDP
poly(U)+1 + phosphate
-
primer required for polymerization
-
r
poly(U)+1 + phosphate
poly(U) + ADP
-
-
-
r
poly(U)+1 + phosphate
poly(U) + ADP
-
-
-
ir
poly(U)+1 + phosphate
poly(U) + ADP
-
-
-
r
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
catalyzes exchange between beta-phosphate of ADP and phosphate, but only in presence of either an oligoribonucleotide bearing an unidentified C-3'-hydroxyl group or of ADP
exchange reaction
-
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
ADP preferred substrate for exchange, little or no reaction occurs with other nucleoside diphosphates
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
ADP, GDP and CDP are better substrates than UDP, IDP and deoxribonucloside diphosphates do not serve as substrate
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
exchange reaction with ADP, CDP, UDP and GDP
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
ribonucleoside 5'-diphosphate + phosphate
ribonucleoside 5'-diphosphate + phosphate
-
-
exchange reaction
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase is involved in tRNA degradation, PNPase is required for efficient 3'-end processing of mRNAs in vivo, but is not sufficient to mediate their degradation, PNPase may function as poly(A) mRNA 3'-5' degrading exonuclease in vivo
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
synthesis of poly(A): no primer addition required if large amounts of enzyme or Mg2+ are used, with small amounts of either component a primer is required, poly(G) synthesis: primer required
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-independent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
arsenolysis of poly(A), poly(C), poly(U) and poly(G)
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
arsenolysis of poly(A), poly(C), poly(U) and poly(G)
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
activity in the absence of a primer, polymerization is stimulated by various polyribonucleotides or RNAs
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
either in the form of a homotrimeric enzyme or associated in a multiprotein complex, the degradosome, PNPase is involved in RNA processing
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase and RNAse II play an essential role in degrading fragments of mRNA generated by prior cleavage by endonucleases
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase accounts for 10% of total mRNA decay, PNPase can bind double stranded DNA, however the affinity is lower than that obtained for both RNA and single stranded DNA binding
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase synthesizes long, highly heteropolymeric poly(A) tails in vivo and accounts for all of the residual polyadenylylation in poly(A) polymerase deficient strains, in addition PNPase is responsible for adding the C and U residues that are found in poly(A) tails in exponentially growing wild-type cultures
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase exonuclease activity plays an essential role in tRNA, mRNA and ribosome metabolism
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase is involved in RNA degradation
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
PNPase specifically binds to 8-oxoguanine-containing RNA, it is suggested that PNPase discriminate between oxidized and normal RNA which my contribute to a high fidelity of translation
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
strong preference for ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
catalyzes addition of a single dAMP from dADP onto an oligoribonucleotide, further addition of either dAMP or AMP to (Ap)ndA is very difficult
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer independent enzyme
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
copolymerization of ADP and dADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
synthetic activity enhanced in presence of a primer
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-independent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
purified enzyme is less dependent on a primer than the enzyme in crude extracts
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-independent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
purified enzyme is less dependent on a primer than the enzyme in crude extracts
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ATP-phosphate exchange at one-third the rate observed with ADP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ADP, GDP and CTP are better substrates than IDP and UDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ADP best substrate, UDP 55%, CDP 51%, IDP 48% of activity with ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ADP best substrate, UDP 55%, CDP 51%, IDP 48% of activity with ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of UDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
chloroplast PNPase is most probably responsible for polyadenylation of RNA
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
-
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
specificity overview
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of IDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of CDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of GDP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-dependent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
polymerization of ADP
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
de novo synthesis of polynucleotides, each of the 4 common ribonucleoside diphosphates can serve separately as a substrate for the polymerization reaction, leading to the formation of homopolymers, polymerization of a mixture of nucleoside diphosphates containing different bases results in the formation of a random copolymer, the enzyme does not require a template and cannot copy one, elongation of a primer oligonucleotide with at least 2 nucleoside residues and a free 3'-terminal hydroxyl group, in the reverse reaction breakdown of polyribonucleotides by phosphorolytic cleavage of the internucleotide bonds
-
r
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-dependent activity
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
ADP, GDP, UDP and CDP polymerized to the extent of 7 S size polymer
-
?
RNAn + a nucleoside diphosphate
RNAn+1 + phosphate
-
primer-dependent activity
-
?
RNAn + UDP
RNAn+1 + phosphate
-
-
-
-
r
RNAn + UDP
RNAn+1 + phosphate
-
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
required for multiple aspects of the 18S rRNA metabolism
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(I)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
PNPase prefers degradation of polyadenylated and polyuridinylated RNAs due to the high binding affinities for poly(A) and poly(U), no activity with polyguanylated RNA
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
processive phosphorolysis of the poly(A) tail of each globin mRNA chain
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(A)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
in addition to its degradative role, PNPase can also function as a polymerase, adding 3' tails to transcripts. The reverse of degradation is favored when nucleoside diphosphate rather than inorganic phosphate is present in excess
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
substrate is synthetic radiolabeled SL9A RNA
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
substrates used for the forward degradation reaction are poly(rA) 15-mer RNA and phosphate
substrates used for the reverse polymerization reaction are poly(rA) 15-mer RNA and ADP
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
in addition to its degradative role, PNPase can also function as a polymerase, adding 3' tails to transcripts. The reverse of degradation is favored when nucleoside diphosphate rather than inorganic phosphate is present in excess
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
substrates used for the forward degradation reaction are poly(rA) 15-mer RNA and phosphate
substrates used for the reverse polymerization reaction are poly(rA) 15-mer RNA and ADP
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(I)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
strong preference for poly(A)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(A)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
enhanced expression of hPNPase(old-35) via a replication-incompetent adenovirus (Ad.hPNPase(old-35)) in human melanoma cells and normal melanocytes results in a characteristic sensecence-like phenotype. Overexpression of hPNPase(old-35) results in increased production of ROS, leading to activation of the nuclear factor (NF)-kappaB pathway. Ad.hPNPase(old-35) infection promotes degradation of IkappaBalpha and nuclear translocation of NF-kappaB and markedly increased binding of the transcriptional activator p50/p65. Infection with (Ad.hPNPase(old-35)) enhances the production of interleukin-6 and interleukin-8, two classical NF-kappaB-responsive cytokines. hPNPase(old-35) might play a significant role in producing pathological changes associated with aging be generating proinflammatory cytokines via ROS and NF-kappaB
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
poly(A) length of human mitochondrial mRNAs is controlled by polyadenylation by poly(A) polymerase and deadenylation by polynucleotide phosphorylase. Polyadenylation is required for stability of mitochondrial mRNAs
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
the enzyme catalyzes the processive phosphorolysis of RNA by using an inorganic phosphate to cleave the phosphodiester linkage at the 3'-end of a RNA chain
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
the functional trimeric phosphorylase is capable of digesting single-stranded RNA to produce final products of about 4 nt in length
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(U)
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
?
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(U)
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(C)
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of RNA
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
enzyme has no nucleoside diphosphate-polymerization activity
-
ir
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(U)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
poly(U) best substrate, yeast RNA 2%, poly(A) 32%, poly(I) 28%, poly(C) 21% of the activity with poly(U)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(I)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(A)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
phosphorolysis of poly(C)
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
poly(A), poly(U) and poly(C) most effective substrates
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
-
-
r
RNAn+1 + phosphate
RNAn + a nucleoside diphosphate
-
PNPase enhances the ability of Yersinia pseudotuberculosis to withstand the killing activities of murine macrophages. PNPase is required for the optimal functioning of the Yersinia type three secretion system, an organelle that injects effector proteins directly into host cells. PNPase plays multifaceted roles in enhancing Yersinia survival in response to stressfull conditions
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is an exoribonuclease
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is an exoribonuclease
-
-
?
additional information
?
-
-
in the presence of Mn2+ and low-level inorganic phosphate, PNPase degrades single-stranded DNA, the limited end-processing of DNA is regulated by ATP and is inactive in the presence of Mg2+ or high-level inorganic phosphate
-
-
?
additional information
?
-
-
in the presence of Mn2+ and low-level inorganic phosphate, PNPase degrades single-stranded DNA, the limited end-processing of DNA is regulated by ATP and is inactive in the presence of Mg2+ or high-level inorganic phosphate
-
-
?
additional information
?
-
-
suppression of Rho-dependent transcription termination within the enzyme gene and its restoration by enzyme protein is an autogenous regulation circuit that modulates enzyme gene expression during cold acclimation
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is essential for growth at low temperatures, while polymerization activity is not essential. RNase PH domains 1 and 2 of polynucleotide phosphorylase are important for its cold shock function, suggesting that the RNase activity of the enzyme is critical for its essential function at low temperature. Its polymerization activity is dispensable in its cold shock function. The RNase R , which is cold inducible, cannot complement the cold shock function of PNPase
-
-
?
additional information
?
-
-
polyribonucleotide phosphorylase-mediated degradation is a major regulatory event controlling the levels of sRNAs, namely stationary phase regulators MicA and RybB, that are required for the accurate expression of outer membrane proteins. Degradation by PNPase surpasses the effect of endonucleolytic cleavages by RNase E. Polyribonucleotide phosphorylase is an important enzyme in the growth phase adaptation to stationary phase
-
-
?
additional information
?
-
regulates its own expression at the level of mRNA stability and translation
-
-
?
additional information
?
-
-
regulates its own expression at the level of mRNA stability and translation
-
-
?
additional information
?
-
-
examination of phosphorolytic activity. Enzyme is able to digest a substrate with a 3' single-stranded tail as well as a substrate possessing a 3' stem-loop structure. Presence of nucleoside diphosphates has no effect on the phosphorolytic activity
-
-
?
additional information
?
-
under conditions of excess nucleoside diphosphate and low concentrations of phosphate, PNPase catalyses the reverse reaction to add 3' extensions to transcripts
-
-
?
additional information
?
-
-
under conditions of excess nucleoside diphosphate and low concentrations of phosphate, PNPase catalyses the reverse reaction to add 3' extensions to transcripts
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is essential for growth at low temperatures, while polymerization activity is not essential. RNase PH domains 1 and 2 of polynucleotide phosphorylase are important for its cold shock function, suggesting that the RNase activity of the enzyme is critical for its essential function at low temperature. Its polymerization activity is dispensable in its cold shock function. The RNase R , which is cold inducible, cannot complement the cold shock function of PNPase
-
-
?
additional information
?
-
-
PNPase specifically binds a synthetic RNA containing the oxidative lesion 8-hydroxyguanine, PNPase binds to RNA molecules of natural sequence that are oxidatively damaged by treatment with hydrogen peroxide, PNPase binds oxidized RNA with higher affinity than untreated RNA of the same sequence
-
-
?
additional information
?
-
-
PNPase specifically binds a synthetic RNA containing the oxidative lesion 8-hydroxyguanine, PNPase binds to RNA molecules of natural sequence that are oxidatively damaged by treatment with hydrogen peroxide, PNPase binds oxidized RNA with higher affinity than untreated RNA of the same sequence
-
-
?
additional information
?
-
-
polyribonucleotide phosphorylase-mediated degradation is a major regulatory event controlling the levels of sRNAs, namely stationary phase regulators MicA and RybB, that are required for the accurate expression of outer membrane proteins. Degradation by PNPase surpasses the effect of endonucleolytic cleavages by RNase E. Polyribonucleotide phosphorylase is an important enzyme in the growth phase adaptation to stationary phase
-
-
?
additional information
?
-
-
enzyme may play a role in excluding oxidized forms of RNA from the translation mechanism
-
-
?
additional information
?
-
-
polynucleotide phosphorylase is involved in protecting cells and limiting damaged RNA under oxidative conditions
-
-
?
additional information
?
-
-
the apoptosis-inducing activity of polynucleotide phosphorylase is mediated by activation of double-stranded RNAdependent protein kinase. Activation of RNA-dependent protein kinase by polynucleotide phosphorylase precedes phosphorylation of eukaryotic initiation factor-2A and induction of growth arrest and DNA damage-inducible gene 153, GADD153, that culminates in the shutdown of protein synthesis and apoptosis. Activation of RNA-dependent protein kinase by polynucleotide phosphorylase also instigates down-regulation of the antiapoptotic protein Bcl-xL
-
-
?
additional information
?
-
-
no activity with ATP nor the other NTPs, as well as mono phosphate nucleotides. Enzyme degrades polyadenylated and nonpolyadenylated RNA at similar rates
-
-
?
additional information
?
-
-
suppressor of Var1 3 and polynucleotide phosphorylase form a 330-kDa heteropentamer that is capable of efficiently degrading double-stranded RNA substrates in the presence of ATP, the hSUV3-PNPase complex prefers substrates containing a 3' overhang and degrades the RNA in a 3'-to-5' directionality
-
-
?
additional information
?
-
-
PNPase, as a phosphorylase, incorporates phosphate and ADP in degradation and polymerization process, respectively. The specificity of the enzyme for the polymerization reaction is high for ADP, with much less activity for other nucleotide diphosphates and no activity for ATP or other nucleotide triphosphates. The human PNPase displays no preferential activity for polyadenylated RNA like bacterial or chloroplast PNPase
-
-
?
additional information
?
-
full-length and DELTAS1 hPNPase cleave the poly(A)12 and poly(U)12 RNA with similar activities and DELTAS1 hPNPase cleaves ssRNA substrate almost as efficiently as full-length PNPase
-
-
?
additional information
?
-
-
full-length and DELTAS1 hPNPase cleave the poly(A)12 and poly(U)12 RNA with similar activities and DELTAS1 hPNPase cleaves ssRNA substrate almost as efficiently as full-length PNPase
-
-
?
additional information
?
-
-
human polynucleotide phosphorylase hPNPaseold-35 is a type I IFN-inducible 3'-5' exoribonuclease, which degrades specific mRNAs and small noncoding RNAs. miR-221, a regulator of the cyclin-dependent kinase inhibitor p27kip1, displays robust downregulation with ensuing up-regulation of p27kip1 by expression of hPNPaseold-35,which also occurs in multiple human melanoma cells upon IFN-beta treatment
-
-
?
additional information
?
-
-
in the cytoplasm, human enzyme, from adenoviral-mediated overexpression, can directly degrade c-myc mRNA by virtue of its 3'-5' exoribonuclease property, and this degradation is specific for c-myc as compared with other mRNAs, such as c-jun, glyceraldehyde 3-phosphate dehydrogenase or GADD 34. In melanoma cells, degradation of microR-221 by hPNPase is more profound compared with other miRNAs
-
-
?
additional information
?
-
PNPase is one of the main exonucleolytic activities involved in RNA turnover and is widely conserved, but PNPase does not seem to be essential for growth, if the organisms are not subjected to special conditions, such as low temperature, transcriptional regulation, overview
-
-
?
additional information
?
-
-
PNPase is one of the main exonucleolytic activities involved in RNA turnover and is widely conserved, but PNPase does not seem to be essential for growth, if the organisms are not subjected to special conditions, such as low temperature, transcriptional regulation, overview
-
-
?
additional information
?
-
PNPase is one of the main exonucleolytic activities involved in RNA turnover and is widely conserved, but PNPase does not seem to be essential for growth, if the organisms are not subjected to special conditions, such as low temperature, transcriptional regulation, overview
-
-
?
additional information
?
-
-
enzyme is involved in tuning the expression of virulence genes and bacterial fitness during infection
-
-
?
additional information
?
-
-
examination of phosphorolytic activity. Enzyme is able to digest a substrate with a 3' single-stranded tail as well as a substrate possessing a 3' stem-loop structure. Presence of nucleoside diphosphates results in decrease of Km value for phosphorolytic activity
-
-
?
additional information
?
-
at the optimal temperature, polynucleotide phosphorylase completely destroys RNAs that possess even a very stable intramolecular secondary structure, but leaves intact RNAs whose 3' end is protected by chemical modification or by hybridization with a complementary oligonucleotide. This allows individual RNAs to be isolated from heterogeneous populations by degrading unprotected species. If oligonucleotide is hybridized to an internal RNA segment, the Tth polynucelotide phosphorylase stalls eight nucleotides downstream of that segment. This allows any arbitrary 5'-terminal fragment of RNA to be prepared with a precision similar to that of run-off transcription, but without the need for a restriction site
-
-
?
additional information
?
-
-
at the optimal temperature, polynucleotide phosphorylase completely destroys RNAs that possess even a very stable intramolecular secondary structure, but leaves intact RNAs whose 3' end is protected by chemical modification or by hybridization with a complementary oligonucleotide. This allows individual RNAs to be isolated from heterogeneous populations by degrading unprotected species. If oligonucleotide is hybridized to an internal RNA segment, the Tth polynucelotide phosphorylase stalls eight nucleotides downstream of that segment. This allows any arbitrary 5'-terminal fragment of RNA to be prepared with a precision similar to that of run-off transcription, but without the need for a restriction site
-
-
?
additional information
?
-
-
enzyme affects the expression and activity of the type III secretion system by distinct mechanisms. the RNA-binding subdomain S1-dependent effect on type III secretion system involves an RNA intermediate
-
-
?
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Ca2+
-
no effect in E. coli enzyme, 0.005 mM, 3fold activation of Bacillus stearothermophilus enzyme
Ca2+
-
no effect in E. coli enzyme, 0.005 mM, 3fold activation of Bacillus stearothermophilus enzyme
Ca2+
-
activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
Cu2+
-
can partially replace Mg2+ in activation
K+
-
-
K+
-
potassium salts activate
K+
-
activates polymerization
K+
-
maximal activation at 200 mm
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
maximal activation of ADP and GDP polymerization at 10 and 5 mM, respectively, inhibition at higher concentrations
Mg2+
-
RNase activity of PNPase requires Mg2+
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
100000 Da form requires high Mg2+ concentrations
Mg2+
essential cofactor for PNPase catalysis
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
activity depends on divalent cation, order of efficiency: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Mg2+
-
required for activity
Mg2+
substituting manganese for magnesium as the metal cofactor enables PNPase to nibble into the DNA tract. A 3'-phosphate group prevents RNA phosphorolysis when the metal cofactor is magnesium
Mg2+
-
required for activity
Mg2+
-
Mg2+ or Mn2+ required for activity, maximal activation at 1 mM Mg2+, inhibition above
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
maximal activation at 6 mM
Mg2+
-
required for activity
Mg2+
-
optimal concentration for polymerization, phosphorolysis and ADP-phosphate exchange at 1 mM, 1-3 mM and 3 mM, respectively
Mg2+
-
divalent cation required, maximal activation at approx. 2 mM, Mg2+ is more effective than Mn2+ for polymerization, Mn2+ better activator in phosphorolytic reaction
Mg2+
-
required for activity
Mg2+
-
optimal concentration for polymerization and phosphorolysis at 0.4 mM, optimum nucleotide/Mg2+ ratios for ADP, CDP and UDP are 4/1, 4/1 and 5/1, respectively
Mg2+
-
required for activity
Mg2+
-
required for activity
Mg2+
-
preferentially activated by Mg2+
Mg2+
-
required for activity
Mg2+
required, enzyme retains significant activity when the concentration is in the micromolar range
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
stimulates polymerization more efficiently than Mg2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
in the presence of Mn2+ and low-level inorganic phosphate, PNPase degrades single-stranded DNA
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
200000 Da form requires Mn2+ for NDP polymerization, polymerization of GDP proceedes efficiently in presence of Mn2+ at 60°C, polymerization with a mutant enzyme from E. coli Q13 requires Mn2+ rather than Mg2+
Mn2+
Mn2+ can substitute for Mg2+ as an essential co-factor for PNPase catalysis
Mn2+
-
manganese can substitute for magnesium as the catalytic metal in PNPase, and RNA degradation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
with manganese as metal cofactor, PNPase can resect an RNA 3'-phosphate end, albeit 80fold slower than a 3'-OH
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
Mg2+ or Mn2+ required for activity, maximal activation at 0.06 mM Mn2+, inhibition above
Mn2+
-
7-9% of activity with Mg2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
optimal concentration for polymerization, phosphorolysis and ADP-phosphate exchange at 1 mM
Mn2+
-
divalent cation required, Mg2+ more effective than Mn2+ for polymerization, Mn2+ better activator in phosphorolytic reaction
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
effective polymer:Mg2+ ratio is 1:1
Mn2+
-
20-30% of activity with Mg2+
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Na+
-
-
Na+
-
activates polymerization
Na+
-
sodium salts activate
Na+
-
NaCl stimulates polymerization maximally at250 mM, inhibition above
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
activity depends on divalent cation, efficiency in descending order: Mg2+, Mn2+, Co2+, Zn2+, Cu2+, Ca2+
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation
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evolution
-
human polynucleotide phosphorylase is an evolutionary conserved RNA-processing enzyme. PNPase contains five motifs that are conspicuously preserved through evolution extending from prokaryotes and plants to mammals. Although hPNPase structurally and biochemically resembles PNPase of other species, overexpression and inhibition studies reveal that hPNPase has evolved to serve more specialized and diversified functions in humans
evolution
-
polynucleotide phosphorylase is a conserved, widely distributed phosphorolytic 3'-5' exoribonuclease
evolution
-
two domains, both resembling closely the phosphorolytic exoribonuclease RNase PH, EC 27.7.56, almost certainly have originated from duplication and fusion of an ancestral gene. While the C-terminal RNase PH-like domain catalyses phosphorolytic attack of RNA, the N-terminal domain has lost this capacity. Instead, it contributes to the ring-like quaternary structure of the trimeric PNPase assembly
evolution
-
two domains, both resembling closely the phosphorolytic exoribonuclease RNase PH, EC 27.7.56, almost certainly have originated from duplication and fusion of an ancestral gene. While the C-terminal RNase PH-like domain catalyses phosphorolytic attack of RNA, the N-terminal domain has lost this capacity. Instead, it contributes to the ring-like quaternary structure of the trimeric PNPase assembly
-
malfunction
-
PNPase-deficient mutant is hypersensitive to oxidative challenges
malfunction
-
deletion of the pnp gene, encoding polynucleotide phosphorylase, results in increased biofilm formation in Escherichia coli
malfunction
-
enzyme depletion decreases splicing efficiency and inhibits intron degradation, effects on intron metabolism, overview. In mutants lacking cpPNPase activity, unusual RNA patterns occur, intron-containing fragments also accumulate in mutants. Mutants show gene-dependent and intermediate RNA phenotypes, suggesting that reduced enzyme activity differentially affects chloroplast transcripts
malfunction
-
in a liver mitochondria from a liver-specific PNPase knockout mouse model, the decrease in functional electron transport chain complexes is responsible for decreased respiration. Liver mitochondria from liver-specific knockout mice display disordered circular and smooth inner membrane criste, similar to mitochondria having impaired components of oxidative phosphorylation pathways. Citrate synthase activity, routinely used as a marker of aerobic capacity, also decreases in the liver of PNPase knockout mice compared with the wild-type mice
malfunction
-
inhibition of the enzyme by shRNA or stable overexpression of miR-221 protects melanoma cells from IFN-beta-mediated growth inhibition
malfunction
-
loss-of-function mutations in pnp result in a decreased stability of several sRNAs including RyhB, SgrS, and CyaR and also decrease both the negative and positive regulation by sRNAs. The defect in stability of CyaR and in negative and positive regulation are suppressed by deletion mutations in RNase E. Lack of sRNA-mediated regulation in the absence of an active form of PNPase is due to the rapid turnover of sRNA resulting from an increase in RNase E activity and/or an increase in access of other ribonucleases to sRNAs. The defect in sRNA regulation caused by the pnp mutations is independent of Hfq. While Hfq does not appear to be limiting, it seems possible that lack of PNPase leads to inactivation of Hfq
malfunction
-
spontaneous mutations resulting from replication errors, which are normally repaired by the mismatch repair system, are sharply reduced in a polynucleotide phosphorylase-deficient Escherichia coli strain
malfunction
-
the inactivation of the pnp gene reduces significantly the ability of Campylobacter jejuni to adhere and to invade Ht-29 cells, the mutant strain exhibits a decrease in swimming ability and chick colonization, 81-176 phenotype, overview. The pnp mutation do not induce profound proteomic changes suggesting that other ribonucleases in the organism might ensure this biological function in the absence of PNPase
malfunction
-
loss-of-function mutations in pnp result in a decreased stability of several sRNAs including RyhB, SgrS, and CyaR and also decrease both the negative and positive regulation by sRNAs. The defect in stability of CyaR and in negative and positive regulation are suppressed by deletion mutations in RNase E. Lack of sRNA-mediated regulation in the absence of an active form of PNPase is due to the rapid turnover of sRNA resulting from an increase in RNase E activity and/or an increase in access of other ribonucleases to sRNAs. The defect in sRNA regulation caused by the pnp mutations is independent of Hfq. While Hfq does not appear to be limiting, it seems possible that lack of PNPase leads to inactivation of Hfq
-
malfunction
-
PNPase-deficient mutant is hypersensitive to oxidative challenges
-
malfunction
-
deletion of the pnp gene, encoding polynucleotide phosphorylase, results in increased biofilm formation in Escherichia coli
-
malfunction
-
enzyme depletion decreases splicing efficiency and inhibits intron degradation, effects on intron metabolism, overview. In mutants lacking cpPNPase activity, unusual RNA patterns occur, intron-containing fragments also accumulate in mutants. Mutants show gene-dependent and intermediate RNA phenotypes, suggesting that reduced enzyme activity differentially affects chloroplast transcripts
-
metabolism
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PNPase, together with the endonuclease RNase E, the DEAD-box RNA helicase RhlB, and enolase, constitutes the RNA degradosome, a multiprotein machine devoted to RNA degradation
metabolism
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the enzyme is involved in RNA degradation and/turnover, major processes controlling RNA levels and important regulators of physiological and pathological processes
metabolism
-
the Krebs cycle metabolite citrate affects the activity of Escherichia coli polynucleotide phosphorylase (PNPase) and, conversely, that cellular metabolism is affected widely by PNPase activity, a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome and on global gene expression, detailed overview
metabolism
-
the Krebs cycle metabolite citrate affects the activity of Escherichia coli polynucleotide phosphorylase (PNPase) and, conversely, that cellular metabolism is affected widely by PNPase activity, a PNPase-mediated response to citrate, and PNPase deletion broadly impacts on the metabolome and on global gene expression, detailed overview
-
metabolism
-
PNPase, together with the endonuclease RNase E, the DEAD-box RNA helicase RhlB, and enolase, constitutes the RNA degradosome, a multiprotein machine devoted to RNA degradation
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physiological function
-
Bacillus subtilis polynucleotide phosphorylase 3'-to-5' DNase activity is involved in DNA repair
physiological function
PNPase is a processive exoribonuclease that contributes to messenger RNA turnover and quality control of ribosomal RNA precursors
physiological function
PNPase is a virulence repressor in benign strains of Dichelobacter nodosus
physiological function
-
PNPase may be solely responsible for chloroplast polyadenylation activity
physiological function
-
PNPase may be solely responsible for chloroplast polyadenylation activity
physiological function
-
PNPase plays a role of in low-temperature survival of Campylobacter jejuni
physiological function
-
PNPase primarily functions in exonucleolytic degradation of RNA in the 3'->5' direction, PNPase also functions in minimizing oxidized RNA in vivo
physiological function
-
PNPase regulates chloroplast transcript accumulation in response to phosphorus starvation, the activity of the chloroplast PNPase is involved in plant acclimation to phosphorus availability and may help maintain an appropriate balance of phosphorus metabolites even under normal growth conditions
physiological function
-
hPNPaseold-35 regulates the expression of specific miRNAs, importance of hPNPaseold-35 induction and miR-221 downregulation in mediating IFN-beta action, mechanism of miRNA regulation involving selective enzymatic degradation, overview
physiological function
human polynucleotide phosphorylase is a 3'-to-5' exoribonuclease that degrades specific mRNA and miRNA, and imports RNA into mitochondria, and thus regulates diverse physiological processes, including cellular senescence and homeostasis
physiological function
-
metabolite-bound PNPase structure and evidence for an allosteric pocket, overview
physiological function
-
pivotal role of PNPase in mitochondrial morphogenesis and respiration in vivo
physiological function
-
polynucleotide phosphorylase is an exoribonuclease that cleaves single-stranded RNA substrates with 3' -5' directionality and processive behaviour
physiological function
-
polynucleotide phosphorylase is an RNA processing enzyme and a component of the RNA degradosome. It plays an important role in RNA processing and turnover, being implicated in RNA degradation and in polymerization of heteropolymeric tails at the 3'-end of mRNA. PNPase is necessary to maintain bacterial cells in the planktonic mode through downregulation of pgaABCD expression and poly-N-acetylglucosamine production. But the pnp gene is not essential. Negative regulation of the poly-N-acetylglucosamine biosynthetic operon pgaABCD by PNPase
physiological function
-
polynucleotide phosphorylase is an RNA-processing enzyme with expanding roles in regulating cellular physiology. By executing exonuclease activity PNPase specifically degrades mature miRNAs, schematic model of microRNA biogenesis and stability, overview. The enzyme might have an essential role in senescence- and differentiation-associated growth inhibition, involvement of hPNPase in producing pathological changes associated with aging by generating pro-inflammatory cytokines via reactive oxygen species and NF-kappaB, growth inhibition in different cancer cells and its molecular mechanism, overview. Direct involvement of PNPase in regulating specific cytosolic RNA import into the mitochondrial matrix, independently of its RNA-processing function
physiological function
-
polynucleotide phosphorylase plays a central role in RNA degradation, generating a pool of ribonucleoside diphosphates that can be converted to deoxyribonucleoside diphosphates by ribonucleotide reductase
physiological function
-
the chloroplastidic enzyme has a major role in maturing mRNA and rRNA 3'-ends, but also participates in RNA degradation through exonucleolytic digestion and polyadenylation.Cchloroplast PNPase and a poly(A) polymerase share the polymerization role in wild-type plants. Chloroplast PNPase appears to be required for a degradation step following endonucleolytic cleavage of the excised lariat. The enzyme functions depend absolutely on the catalytic site within the second duplicated RNase PH domain, and appear to be modulated by the first RNase PH domain, but both PNPase domains contribute to chloroplast rRNA and mRNA processing, overview
physiological function
-
the role of PNPase is pleiotropic
physiological function
deletion of the gene encoding PNPase leads to hyperaggregation and increased adhesion to epithelial cells. The aggregation induced is dependent on pili and mediated by excessive pilus bundling. PNPase expression is induced following bacterial attachment to human cells. Deletion of PNPase leads to global transcriptional changes and the differential regulation of 469 genes. PNPase is required for full virulence in an in vivo model of N. meningitidis infection
physiological function
-
in vitro, enzyme forms a ternary complex comprised of PNPase, chaperine Hfq, and sRNA and PNPase and Hfq may also form a ribonucleoprotein complex in the cell. In in vitro studies, PNPase readily degrades sRNAs in the absence of Hfq, but binds and is unable to degrade sRNAs in its presence
physiological function
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mutations in PNPase residues predicted to be involved in RNase Y binding show a loss of PNPase-RNase Y interaction. For the two mRNAs investigated, disruption of the PNPase-RNase Y interaction does not appear to affect mRNA turnover
physiological function
PNPase discriminates RNA versus DNA during the 3' phosphorolysis reaction. A kinetic block to 3' phosphorolysis of a DNA tract within an RNA polynucleotide is exerted when resection has progressed to the point that a 3' monoribonucleotide flanks the impeding DNA segment. The position of the pause one nucleotide upstream of the first deoxynucleotide encountered is independent of DNA tract length. The duration of the pause is affected by DNA tract length, being transient for a single deoxynucleotide and durable when two or more consecutive deoxynucleotides are encountered
physiological function
PNPase forms a complex with RNase E. An extremely conserved nonapeptide (RRRRRRSSA) located near the very end of RNase E, serves as the PNPase recognition site in both the filamentous cyanobacterium Anabaena sp. PCC7120 and the unicellular cyanobacterium Synechocystis sp. PCC6803
physiological function
PNPase forms a complex with RNase E. An extremely conserved nonapeptide (RRRRRRSSA) located near the very end of RNase E, serves as the PNPase recognition site in both the filamentous cyanobacterium Anabaena sp. PCC7120 and the unicellular cyanobacterium Synechocystis sp. PCC6803
physiological function
the cvfA-deletion mutant phenotype showing decreased agr expression and hemolysin production, is suppressed by disrupting pnpA-encoding PNPase. Loss of the 3'- to 5'-exonuclease activity is required for suppression. CvfA protein hydrolyzes a 2',3'-cyclic phosphodiester bond at the RNA 3' terminus, producing RNA with a 3'-phosphate. Purified PNPase efficiently degrades RNA with 2',3'-cyclic phosphate at the 3' terminus (2',3'-cyclic RNA), but it inefficiently degrades 3'-phosphorylated RNA
physiological function
-
the KH-S1 domains of PNPase are required for the type III secretion system (T3SS) and bacterial virulence. PNPase shows a pleiotropic role in gene regulation. The RNA level of exsA is decreased in a mutant lacking the KH-S1 domains. The pilus biosynthesis genes are down regulated and the type VI secretion system (T6SS) genes are up regulated in the mutant, which is caused by increased levels of small RNAs, RsmY, and RsmZ. Deletion of the KH-S1 domains does not affect the transcription of RsmY/Z, but increases their stabilities
physiological function
-
the Pnp gene is required for Salmonella typhimurium virulence and gastrointestinal colonization of the natural swine host. Following intranasal inoculation, a significant increase in rectal temperature is observed in the pigs inoculated with wild-type Salmonella typhimurium compared to the pigs inoculated with the Pnp mutant. Fecal shedding of the Pnp mutant is significantly reduced during the 7-day study compared to the wild-type strain. Tissue colonization is also significantly reduced in the pigs inoculated with the pnp mutant, including the tonsils, ileocecal lymph nodes, Peyer's Patch region of the ileum, cecum and contents of the cecum
physiological function
compared to the wild type, the production of fengycin in mutant strains lacking PNPase activity has decreased by about 70-40%, and its antifungal activity towards the plant pathogen Botrytis cinerea is hampered
physiological function
in cardiac tissue from human and mouse models of type 2 diabetes mellitus, levels of Argonaute2 protein, associated with cytosolic and mitochondrial miRNAs, are unchanged while PNPase protein expression levels are increased. There an increase in the association between both proteins in the diabetic state
physiological function
mutation of the polynucleotide phosphorylase coding gene pnp increases the bacterial resistance to ciprofloxacin.The expression of pyocin biosynthesis genes is decreased in the pnp mutant. PrtR, a negative regulator of pyocin biosynthesis genes, is upregulated in the pnp mutant. Polynucleotide phosphorylase represses the expression of PrtR on the posttranscriptional level. A fragment containing 43 nucleotides of the 5' untranslated region is involved in the polynucleotide phosphorylase mediated regulation of PrtR
physiological function
mutation of the polynucleotide phosphorylase encoding gene increases bacterial tolerance to aminoglycoside antibiotics. The upregulation of the multidrug efflux pump MexXY genes is responsible for the increased tolerance of the polynucleotide phosphorylase mutant. Polynucleotide phosphorylase controls the translation of the armZ mRNA, which regulates the expression of MexXY through its 59 untranslated region
physiological function
PNPase forms a complex with RNase J1 and RNase J2 without substantially altering either exo-ribonuclease or polyadenylation activity of the enzyme
physiological function
PNPase is a contributor to mitochondrial miRNA import through the transport of miRNA-378, which may regulate bioenergetics during type 2 diabetes mellitus. In cardiac tissue from human and mouse models of type 2 diabetes mellitus, levels of Argonaute2 protein, associated with cytosolic and mitochondrial miRNAs, are unchanged while PNPase protein expression levels are increased. There an increase in the association between both proteins in the diabetic state. miRNA-378 is significantly increased in db/db mice, leading to decrements in ATP6 levels and ATP synthase activity, which is also exhibited when overexpressing PNPase in HL-1 cardiomyocytes
physiological function
polynucleotide phosphorylase and endo-type RNases, RNase E/G and YbeY, are involved in the 3' maturation of 4.5S RNA in Corynebacterium glutamicum. The mature form of 4.5S RNA is inefficiently formed in RNase E/G/polynucleotide phosphorylase mutant cells. Immunoprecipitated Ffh protein of the signal recognition particle contains immature 4.5S RNA in RNase E/G, in polynucleotide phosphorylase and in mutants RNase YbeY mutants
physiological function
polynucleotide phosphorylase and RNase PH interact to support sRNA stability, activity, and base pairing in exponential and stationary growth conditions. They facilitate the stability and regulatory function of the sRNAs RyhB, CyaR, and MicA during exponential growth. Polynucleotide phosphorylase may contribute to pairing between RyhB and its mRNA targets. During stationary growth, each sRNA responds differently to the absence or presence of PNPase and RNase PH. Polynucleotide phosphorylase and RNase PH stabilize only Hfq-bound sRNAs
physiological function
polynucleotide phosphorylase contributes to the degradation of specific short mRNA fragments, the majority of which bind RNA chaperone Hfq and are derived from targets of sRNAs. The mRNA-derived fragments accumulate in the absence of polynucleotide phosphorylase or its exoribonuclease activity and interact with polynucleotide phosphorylase. Mutations in chaperone Hfq or in the seed pairing region of some sRNAs eliminate the requirement of polynucleotide phosphorylase for their stability
physiological function
-
polynucleotide phosphorylase enhances both homologous recombination upon P1 transduction and error prone DNA repair of double strand breaks induced by radiomimetic zeocin. Homologous recombination does not require polynucleotide phosphorylasephosphorolytic activity and is modulated by its RNA binding domains whereas error prone DNA repair of zeocin-induced DNA damage is dependent on polynucleotide phosphorylase catalytic activity and cannot be suppressed by overexpression of RNase II. Polynucleotide phosphorylase mutants are more sensitive than the wild-type to zeocin. This phenotype depends on polynucleotide phosphorylasephosphorolytic activity and is suppressed by RNase II
physiological function
polynucleotide phosphorylase is involved in controlling the levels of RNA oxidation marker 8-hydrooxyguanosine in both cytoplasmic and mitochondrial fractions. Expression of exogenous polynucleotide phosphorylase reduces 8-hydrooxyguanosine levels in both cytoplasm and mitochondria. The S1 RNA binding domain is crucial for reducing 8-hydrooxyguanosine in both cytoplasm and mitochondria, while the N-terminal mitochondrial translocation signal is required for 8-hydrooxyguanosine reduction in mitochondria. One of the RPH1 or RPH2 domains is sufficient to reduce 8-hydrooxyguanosine levels in RNA under oxidative stress conditions
physiological function
-
compared to the wild type, the production of fengycin in mutant strains lacking PNPase activity has decreased by about 70-40%, and its antifungal activity towards the plant pathogen Botrytis cinerea is hampered
-
physiological function
-
polynucleotide phosphorylase is an exoribonuclease that cleaves single-stranded RNA substrates with 3' -5' directionality and processive behaviour
-
physiological function
-
mutations in PNPase residues predicted to be involved in RNase Y binding show a loss of PNPase-RNase Y interaction. For the two mRNAs investigated, disruption of the PNPase-RNase Y interaction does not appear to affect mRNA turnover
-
physiological function
-
PNPase primarily functions in exonucleolytic degradation of RNA in the 3'->5' direction, PNPase also functions in minimizing oxidized RNA in vivo
-
physiological function
-
Bacillus subtilis polynucleotide phosphorylase 3'-to-5' DNase activity is involved in DNA repair
-
physiological function
-
deletion of the gene encoding PNPase leads to hyperaggregation and increased adhesion to epithelial cells. The aggregation induced is dependent on pili and mediated by excessive pilus bundling. PNPase expression is induced following bacterial attachment to human cells. Deletion of PNPase leads to global transcriptional changes and the differential regulation of 469 genes. PNPase is required for full virulence in an in vivo model of N. meningitidis infection
-
physiological function
-
PNPase forms a complex with RNase E. An extremely conserved nonapeptide (RRRRRRSSA) located near the very end of RNase E, serves as the PNPase recognition site in both the filamentous cyanobacterium Anabaena sp. PCC7120 and the unicellular cyanobacterium Synechocystis sp. PCC6803
-
physiological function
-
metabolite-bound PNPase structure and evidence for an allosteric pocket, overview
-
physiological function
-
polynucleotide phosphorylase is an RNA processing enzyme and a component of the RNA degradosome. It plays an important role in RNA processing and turnover, being implicated in RNA degradation and in polymerization of heteropolymeric tails at the 3'-end of mRNA. PNPase is necessary to maintain bacterial cells in the planktonic mode through downregulation of pgaABCD expression and poly-N-acetylglucosamine production. But the pnp gene is not essential. Negative regulation of the poly-N-acetylglucosamine biosynthetic operon pgaABCD by PNPase
-
physiological function
-
the chloroplastidic enzyme has a major role in maturing mRNA and rRNA 3'-ends, but also participates in RNA degradation through exonucleolytic digestion and polyadenylation.Cchloroplast PNPase and a poly(A) polymerase share the polymerization role in wild-type plants. Chloroplast PNPase appears to be required for a degradation step following endonucleolytic cleavage of the excised lariat. The enzyme functions depend absolutely on the catalytic site within the second duplicated RNase PH domain, and appear to be modulated by the first RNase PH domain, but both PNPase domains contribute to chloroplast rRNA and mRNA processing, overview
-
physiological function
-
PNPase forms a complex with RNase J1 and RNase J2 without substantially altering either exo-ribonuclease or polyadenylation activity of the enzyme
-
physiological function
-
polynucleotide phosphorylase and endo-type RNases, RNase E/G and YbeY, are involved in the 3' maturation of 4.5S RNA in Corynebacterium glutamicum. The mature form of 4.5S RNA is inefficiently formed in RNase E/G/polynucleotide phosphorylase mutant cells. Immunoprecipitated Ffh protein of the signal recognition particle contains immature 4.5S RNA in RNase E/G, in polynucleotide phosphorylase and in mutants RNase YbeY mutants
-
additional information
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also see for EC 2.7.7.56. RNase PH, EC 2.7.7.8, consists of tandem N-terminal RNase PH-like segments, known as core domains, as well as KH and S1 RNA-binding domains. The conserved residue D625 is located in the catalytic site and functions in phosphorolysis
additional information
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human melanoma cells infected with an adenovirus expressing hPNPaseold-35 and are used for identification of miRNAs differentially and specifically regulated by hPNPaseold-35. Overexpression of miR-221 in HO-1 cells confers resistance to IFN-beta-mediated growth arrest
additional information
the C-terminal S1 domain is not critical for RNA binding, and conversely, the conserved GXXG motif in the KH domain directly participates in RNA binding in hPNPase. The enzyme uses a KH pore to trap a long RNA 3' tail that is further delivered into an RNase PH channel for the degradation process. The three KH domains form a KH pore situated on the top of the hexameric ring-like structure. The KH pore extends the central channel formed by the RNase PH domains and is involved in the binding of RNA substrates, which are further delivered to the active site located within the central channel. Structural RNA with short 3' tails are, on the other hand, transported but not digested by hPNPase. Structural model of hPNPase, overview
additional information
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the C-terminal S1 domain is not critical for RNA binding, and conversely, the conserved GXXG motif in the KH domain directly participates in RNA binding in hPNPase. The enzyme uses a KH pore to trap a long RNA 3' tail that is further delivered into an RNase PH channel for the degradation process. The three KH domains form a KH pore situated on the top of the hexameric ring-like structure. The KH pore extends the central channel formed by the RNase PH domains and is involved in the binding of RNA substrates, which are further delivered to the active site located within the central channel. Structural RNA with short 3' tails are, on the other hand, transported but not digested by hPNPase. Structural model of hPNPase, overview
additional information
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the enzyme has a ring-like, trimeric architecture that creates a central channel where phosphorolytic active sites reside, with asymmetry within the catalytic core of the enzyme. One face of the ring is decorated with RNA-binding K-homology (KH) and S1 domains. In the RNA-free form, the S1 domains adopt a splayed conformation that may facilitate capture of RNA substrates. In the RNA-bound structure, the three KH domains collectively close upon the RNA and direct the 3' end towards a constricted aperture at the entrance of the central channel. Structural non-equivalence, induced upon RNA binding, helps to channel substrate to the active sites through mechanical ratcheting. Access to the PNPase active sites is through the central channel, which can accommodate single-stranded RNA with some structural adjustment of a constricted aperture at the channel entrance, residues and motifs involved in RNA directionality, recognition, and quarternary changes in the core, structure-function-relationship, detailed overview
additional information
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the increase in the rNDP pools generated by polynucleotide phosphorylase degradation of RNA is responsible for the spontaneous mutations observed in an mismatch repair-deficient background, and is also responsible for the observed mutations in the mutT mutator background and those that occur after treatment with 5-bromodeoxyuridine
additional information
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the S1 and KH domains of polynucleotide phosphorylase determine the efficiency of RNA binding and enzyme autoregulation, modeling of the roles of the KH and S1 domains in PNPase-RNA interactions and in substrate binding, overview
additional information
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two conserved catalytic RNase PH regions, a small domain of about 250 amino acid residues involved primarily in the 3' processing of transfer RNA precursors, are present at the N-terminus of the human enzyme. The RNA-binding property of hPNPase is conferred by two C-terminal RNA-binding domains, KH and S1
additional information
-
the enzyme has a ring-like, trimeric architecture that creates a central channel where phosphorolytic active sites reside, with asymmetry within the catalytic core of the enzyme. One face of the ring is decorated with RNA-binding K-homology (KH) and S1 domains. In the RNA-free form, the S1 domains adopt a splayed conformation that may facilitate capture of RNA substrates. In the RNA-bound structure, the three KH domains collectively close upon the RNA and direct the 3' end towards a constricted aperture at the entrance of the central channel. Structural non-equivalence, induced upon RNA binding, helps to channel substrate to the active sites through mechanical ratcheting. Access to the PNPase active sites is through the central channel, which can accommodate single-stranded RNA with some structural adjustment of a constricted aperture at the channel entrance, residues and motifs involved in RNA directionality, recognition, and quarternary changes in the core, structure-function-relationship, detailed overview
-
additional information
-
also see for EC 2.7.7.56. RNase PH, EC 2.7.7.8, consists of tandem N-terminal RNase PH-like segments, known as core domains, as well as KH and S1 RNA-binding domains. The conserved residue D625 is located in the catalytic site and functions in phosphorolysis
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D625N
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naturally occuring mutation in the catalytic site, inactive mutant
G596R
-
naturally occuring mutation near the catalytic domain, inactive mutant. Mutant G596R fails to fold correctly, perhaps as a consequence of its inability to bind phosphate, and is thus marked for degradation
D625N
-
naturally occuring mutation in the catalytic site, inactive mutant
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G596R
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naturally occuring mutation near the catalytic domain, inactive mutant. Mutant G596R fails to fold correctly, perhaps as a consequence of its inability to bind phosphate, and is thus marked for degradation
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D323A
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weakening of interaction with RNase Y. Asp-323 sits near the C-terminal end of the RNase Y peptide sequence
E331A
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loss of interaction with RNase Y. The Glu-331 side faces the helical domain of the RNase Y peptide
R35A
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weakening of interaction with RNase Y. The Arg35 side chain faces the non-helical domain of the binding peptide
R546A
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weakening of interaction with RNase Y. Arg546 is located farther away from the binding peptide
D323A
-
weakening of interaction with RNase Y. Asp-323 sits near the C-terminal end of the RNase Y peptide sequence
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E331A
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loss of interaction with RNase Y. The Glu-331 side faces the helical domain of the RNase Y peptide
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R35A
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weakening of interaction with RNase Y. The Arg35 side chain faces the non-helical domain of the binding peptide
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R546A
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weakening of interaction with RNase Y. Arg546 is located farther away from the binding peptide
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C1310T
-
mutation invovled in sRNA regulation defects
C277T
-
mutation invovled in sRNA regulation defects
C943T
-
mutation invovled in sRNA regulation defects
DELTA549-709
complementation of growth defect at 15°C of host strain
F635A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
F635A/F638A/H650A
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site-directed mutagenesis, the mutant enzyme shows highly reduced activity and an increased RNA binding constant compared to the wild-type enzyme
F635R/F638R/H650R
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
F638A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
G1307A
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mutation invovled in sRNA regulation defects
G1466A
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mutation invovled in sRNA regulation defects
G570C
-
site-directed mutagenesis, the mutant enzyme shows highly reduced activity and an increased RNA binding constant compared to the wild-type enzyme
G570C/V679A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
H650A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
I555T
-
site-directed mutagenesis, the mutant enzyme shows slightly reduced activity compared to the wild-type enzyme
I576A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
I576A/F638A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
I576T
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
I576T/F638A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
I576T/T585A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
K571L
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
K571Q
-
site-directed mutagenesis, the mutant enzyme shows reduced activity and an increased RNA binding constant compared to the wild-type enzyme
R100D
-
growth at 37°C, not able to grow at 15°C
R153A/R372A/R405A/R409A
-
site-directed mutagenesis
R319H
-
growth at 37°C, not able to grow at 15°C
R398D/R399D
-
growth at 37°C, not able to grow at 15°C
R83A
the mutation has little apparent effect on activity but causes the full-length PNPase to stall on RNA oligomers shorter than eight nucleotides
W233Stop
complementation of growth defect at 15°C of host strain
R100D
-
growth at 37°C, not able to grow at 15°C
-
R319H
-
growth at 37°C, not able to grow at 15°C
-
R398D/R399D
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growth at 37°C, not able to grow at 15°C
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C1310T
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mutation invovled in sRNA regulation defects
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C277T
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mutation invovled in sRNA regulation defects
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C943T
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mutation invovled in sRNA regulation defects
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G1307A
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mutation invovled in sRNA regulation defects
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R153A/R372A/R405A/R409A
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site-directed mutagenesis
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D135G
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unlike trimeric wild-type, mutant is monomeric. Almost complete inhibition of degradation and polyadenylation activities
D544G
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decrease in degradation activity, increase in polymerization
G622D
site-directed mutagenesis
D526A
mutation of the full-length and S1-domain deletion PNPases does not affect manganese- or magnesisum-dependent binding to RNA
D526A/D532A
mutation of the full-length and S1-domain deletion PNPases does not affect manganese-or magnesium-dependent binding to RNA
S441A
catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure
S442A
catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure
S443A
catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure
S441A
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catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure
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S442A
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catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure
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S443A
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catalytically inactive, mutation does not alter the secondary structural content or the quaternary structure
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A552T
complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance
A552T
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.7, as compared with 1.0 in wild-type
E371K
complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance
E371K
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type
E81D
complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity
E81D
impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 1.6, as compared with 1.0 in wild-type
E81K
complementation of growth defect at 15°C of host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity
E81K
impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.4, as compared with 1.0 in wild-type
P98L
complementation of growth defect at 15°C of host strain, forms of smaller colonies than host strain. Severe reduction of enzyme activity and increased PNPase expression levels
P98L
impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.03, as compared with 1.0 in wild-type
R97C
complementation of growth defect at 15°C of host strain. Severe reduction of enzyme activity and increased PNPase expression levels
R97C
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.1, as compared with 1.0 in wild-type
V304A/V305D
complementation of growth defect at 15°C of host strain
V304A/V305D
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.02, as compared with 1.0 in wild-type
V521I
complementation of growth defect at 15°C of host strain. Modest effect of mutation on phosphorolytic activity and protein abundance
V521I
ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.5, as compared with 1.0 in wild-type
V639D
complementation of growth defect at 15°C of host strain, migrates slower than wild-type on SDS-PAGE, forms of smaller colonies than host strain. Increase in PNPase abundance without significantly impairing phosphorolytic activity
V639D
impaired growth at 15°C, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type
additional information
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construction of a pnp inactivation mutant, comparative proteomic analysis and 81-176 phenotype, overview. Levels of peb3 and katA mRNA are significantly decreased in the pnp mutant strain compared to the parental strain, while gene expression of luxS and hsp90 remains unaffected by the pnp mutation, but not protein expression, overview. Poly(A) degradation by lysates of the pnp mutant strain is almost totally non-responsive to phosphate addition
additional information
construction of hybrid proteins by replacing the S1 RNA binding domain of RNase II for the S1 from enzyme. PNPase S1 domain can partially restore the RNA-binding ability and exonucleolytic activity of Rnase II and is able to induce the trimerization of the Rnase II-PNPase hybrid protein
additional information
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construction of hybrid proteins by replacing the S1 RNA binding domain of RNase II for the S1 from enzyme. PNPase S1 domain can partially restore the RNA-binding ability and exonucleolytic activity of Rnase II and is able to induce the trimerization of the Rnase II-PNPase hybrid protein
additional information
C-terminal KH/S1 domain truncated mutant, crystallization data. Mutant binds and cleaves RNA less efficiently with an 8fold reduced binding affinity and forms a less stable trimer. Mutation of Arg-residues in the central channel neck region produces defective enzymes that either bind and cleave RNA less efficiently or generate longer cleaved oligonucleotide products
additional information
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C-terminal KH/S1 domain truncated mutant, crystallization data. Mutant binds and cleaves RNA less efficiently with an 8fold reduced binding affinity and forms a less stable trimer. Mutation of Arg-residues in the central channel neck region produces defective enzymes that either bind and cleave RNA less efficiently or generate longer cleaved oligonucleotide products
additional information
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deletion of KHS1 domain, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type. Deletion mutant lacking amino acids 549-709, no growth at 15°C. Both first and second core domains are involved in the catalysis of the phosphorolytic reaction, and both phosphorolytic activity and RNA binding are required for autogenous regulation and growth in the cold
additional information
deletion of KHS1 domain, ratio of phosphorolytic activity to polynucleotide phosphorylase activity 0.6, as compared with 1.0 in wild-type. Deletion mutant lacking amino acids 549-709, no growth at 15°C. Both first and second core domains are involved in the catalysis of the phosphorolytic reaction, and both phosphorolytic activity and RNA binding are required for autogenous regulation and growth in the cold
additional information
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in a mutant lacking polyribonucleotide phosphorylase activity, the pattern of outer membrane proteins is changed. In stationary phase, stationary phase regulator MicA RNA levels are increased in the mutant, leading to a decrease in the levels of its target ompA mRNA and the respective protein
additional information
several new pnp alleles constructed. To identify specific cis-acting determinants of PNPase autoregulation and discriminate between the two proposed models, several pnpL DELTApnp-871 mutants and one DELTApnp-1010t DELTApnp-871 chromosomal double mutant are constructed
additional information
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several new pnp alleles constructed. To identify specific cis-acting determinants of PNPase autoregulation and discriminate between the two proposed models, several pnpL DELTApnp-871 mutants and one DELTApnp-1010t DELTApnp-871 chromosomal double mutant are constructed
additional information
study on the effect of specific mutations in the two RNA binding domains KH and S1. Removal of critical motifs that stabilize the hydrophobic core of each domain, as well as a complete deletion of both severely impaireds binding to RNA. all mutants are enzymatically active but display significant changes in the kinetic behaviour of both phosphorolysis and polymerization activities. Mutants do not autoregulate efficiently and are unable to complement the growth defect of a chromosomal enzmye deletion at 18°C
additional information
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study on the effect of specific mutations in the two RNA binding domains KH and S1. Removal of critical motifs that stabilize the hydrophobic core of each domain, as well as a complete deletion of both severely impaireds binding to RNA. all mutants are enzymatically active but display significant changes in the kinetic behaviour of both phosphorolysis and polymerization activities. Mutants do not autoregulate efficiently and are unable to complement the growth defect of a chromosomal enzmye deletion at 18°C
additional information
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construction of a strain in which PNPase activity is uncoupled from the degradosome through the deletion of the C-terminal degradosome-scaffold-ing domain of RNase E. Compared with the parental strain, significant differences are distributed across many metabolic pathways, including the Krebs cycle, amino acid synthesis, and glycolysis in the mutant strain. Salient differences are seen for amino acids and increases in the concentrations of succinate, fumarate, and malate, suggesting uncoupling of the two halves of the Krebs cycle
additional information
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construction of domain deletion mutants DELTAKH DELTAS1, DELTAKH, and DELTAS1
additional information
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deletion of gene pnp in Eschericchia coli strain C-1a leading to strong cell aggregation in liquid medium dependent on the extracellular polysaccharide poly-N-acetylglucosamine. Operon pgaABCD transcript levels are increased in the pnp mutant compared to the wild-type enzyme. Inactivation of the pnp gene induces poly-N-acetylglucosamine production. The aggregative phenotype of the C-5691 (DELTApnp) strain is complemented by basal expression from a multicopy plasmid of the pnp gene under araBp promoter, overview
additional information
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genetic selection and screen for mutants defective in the post-transcriptional regulation of gene expression by sRNAs, i.e. CyaR, SgrS, and RyhB. Each of the pnp mutations isolated, as well as a pnp deletion, are transduced into strain DJ624, overview. The defect in sRNA regulation caused by the pnp mutations is independent of Hfq. While Hfq does not appear to be limiting, it seems possible that lack of PNPase leads to inactivation of Hfq
additional information
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genetic selection and screen for mutants defective in the post-transcriptional regulation of gene expression by sRNAs, i.e. CyaR, SgrS, and RyhB. Each of the pnp mutations isolated, as well as a pnp deletion, are transduced into strain DJ624, overview. The defect in sRNA regulation caused by the pnp mutations is independent of Hfq. While Hfq does not appear to be limiting, it seems possible that lack of PNPase leads to inactivation of Hfq
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additional information
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construction of a strain in which PNPase activity is uncoupled from the degradosome through the deletion of the C-terminal degradosome-scaffold-ing domain of RNase E. Compared with the parental strain, significant differences are distributed across many metabolic pathways, including the Krebs cycle, amino acid synthesis, and glycolysis in the mutant strain. Salient differences are seen for amino acids and increases in the concentrations of succinate, fumarate, and malate, suggesting uncoupling of the two halves of the Krebs cycle
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additional information
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deletion of gene pnp in Eschericchia coli strain C-1a leading to strong cell aggregation in liquid medium dependent on the extracellular polysaccharide poly-N-acetylglucosamine. Operon pgaABCD transcript levels are increased in the pnp mutant compared to the wild-type enzyme. Inactivation of the pnp gene induces poly-N-acetylglucosamine production. The aggregative phenotype of the C-5691 (DELTApnp) strain is complemented by basal expression from a multicopy plasmid of the pnp gene under araBp promoter, overview
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additional information
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in a mutant lacking polyribonucleotide phosphorylase activity, the pattern of outer membrane proteins is changed. In stationary phase, stationary phase regulator MicA RNA levels are increased in the mutant, leading to a decrease in the levels of its target ompA mRNA and the respective protein
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additional information
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depletion of enzyme by RNAi approach or overexpression of c-myc protects melanoma cells from interferon-beta mediated grwoth inhibition. Targeted overexpression of enzyme as a therapeutic strategy for c-myc overexpressing and interferon-beta resisitant tumors
additional information
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enzyme depletion using RNAi does not affect mitochondrial RNA levels but impairs mitochondrial electrochemical membrane potential, decreases respiratory chain activity and correlates with altered mitochondrial morphology. This results in F0F1-ATP synthase instability, impaired ATP generation, lactate accumulation, and AMP kinase phosphorylation with reduced cell proliferation
additional information
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overexpression of polynucleotide phosphorylase in HeLa cells under oxidative stress conditions reduces RNA oxidation and increases cell viability against H2O2 insult. Knock-down of enzyme decreases viability and increases 8-oxoguanosine levels in cells exposed to H2O2
additional information
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stable silencing by establishing HeLa cell lines expressing shRNA. Silencing significantly affects processing and polyadenylation of mitochondrial mRNAs with different effects on different genes. The stable poly(A) tails at the 3' ends of COX1 transcripts are abolished, while COX3 poly(A) tails remain unaffected and ND5 and ND3 poly(A) extensions increase in length. Despite the lack of polyadenylation at the 3' end, COX1 mRNA and protein accumulate to normal levels, as is the case for all 13 mitochondria-encoded proteins. ATP depletion also alters poly(A) tail length
additional information
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the promoter of Progression Elevated Gene-3 functions selectively in a diverse array of human cancer cells. An adenovirus constructed with the Progression Elevated Gene-3 promoter driving expression of polyribonucleotide phosphorylase containing a C-terminal hemaglutinin-tag induces robust transgene expression, growth suppression, apoptosis, and cell-cycle arrest in a broad panel of pancreatic cancer cells
additional information
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upon expression in Escherichia coli, human enzyme does not form hetero-complexes with Escheichia coli enzyme
additional information
generation of a S1 domain-lacking mutant enzyme, domain organization of full-length and S1 domain-truncated hPNPase. overview. Full-length and DELTAS1 hPNPase cleave the poly(A)12 and poly(U)12 RNA with similar activities and DELTAS1 hPNPase cleaves ssRNA substrate almost as efficiently as full-length PNPase
additional information
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generation of a S1 domain-lacking mutant enzyme, domain organization of full-length and S1 domain-truncated hPNPase. overview. Full-length and DELTAS1 hPNPase cleave the poly(A)12 and poly(U)12 RNA with similar activities and DELTAS1 hPNPase cleaves ssRNA substrate almost as efficiently as full-length PNPase
additional information
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human melanoma cells are infected with empty adenovirus or with an adenovirus expressing hPNPaseold-35 and identification of miRNAs differentially and specifically regulated by hPNPaseold-35
additional information
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targeted overexpression of hPNPase represents a strategy to selectively downregulate RNA expression and consequently intervene in a variety of pathophysiological conditions, enzyme silencing in PNPase RNA interference-transfected HEK293 cells
additional information
expression of polynucleotide phosphorylase mutants lacking specific functional domains, i.e., mitochondrial translocation signal (MTS), catalytic domains (RPH1 and RPH2) and RNA binding domains (KH and S1), in cultured HeLa cells. MTS is required for polynucleotide phosphorylase to reduce 8-hydrooxyguanosine in mitochondria, but not in cytoplasm. Both RPH1 or RPH2 domain alone are able to support the full activity of polynucleotide phosphorylase in reducing 8-hydrooxyguanosine during oxidative stress, and the S1 RNA-binding domain, but not KH, is required for polynucleotide phosphorylase to reduce 8-hydrooxyguanosine under oxidative stress
additional information
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expression of polynucleotide phosphorylase mutants lacking specific functional domains, i.e., mitochondrial translocation signal (MTS), catalytic domains (RPH1 and RPH2) and RNA binding domains (KH and S1), in cultured HeLa cells. MTS is required for polynucleotide phosphorylase to reduce 8-hydrooxyguanosine in mitochondria, but not in cytoplasm. Both RPH1 or RPH2 domain alone are able to support the full activity of polynucleotide phosphorylase in reducing 8-hydrooxyguanosine during oxidative stress, and the S1 RNA-binding domain, but not KH, is required for polynucleotide phosphorylase to reduce 8-hydrooxyguanosine under oxidative stress
additional information
construction of gene pnp deletion mutants, the mutants do not exhibit cold sensitivity, phenotype, overview
additional information
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construction of gene pnp deletion mutants, the mutants do not exhibit cold sensitivity, phenotype, overview
additional information
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construction of gene pnp deletion mutants, the mutants do not exhibit cold sensitivity, phenotype, overview
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additional information
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enzyme inactivation strain, PNPase deficiency results in increased expression of salmonella plasmid virulence genes. Six genes are significantly upregulated, including spvABC, rtcB, entC, and STM2236. A growth advantage of the mutant strain in BALB/c mice depends on plasmid virulence gene spvR as well
additional information
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enzyme deletion strain is less virulent in mouse than the isogenic wild-type. Enzyme deletion strains show enhanced levels of type III secretion system T3SS encoding transcripts and proteins. T3SS expression levels do not differ between enzyme deletion strains expressing active and inactive S1 RNA binding domain of enzyme which is required for normal T3SS activity
additional information
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polynucleotide phosphorylase deletion strain is less virulent in mouse compared with the isogenic wild-type strain. Deletion strains possess enhanced levels of type III secretion system-encoding transcripts and proteins. A S1 variant of polynucleotide phosphorylase containing a disruption in its RNA-binding subdomain cannot restore normal type III secretion system activity
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