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32P-labeled partial duplex DNA bound to nitrocellulose membranes
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the enzyme unwinds DNA in the 5'-3' direction in relation to the strand to which it binds and has an absolute necessity for single-stranded regions of DNA for the ATPase activity
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61-nucleotide DNA
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ATP + H2O
ADP + phosphate
CTP + H2O
CDP + phosphate
dATP + H2O
dADP + phosphate
dCTP + H2O
dCDP + phosphate
dGTP + H2O
dGDP + phosphate
double-stranded DNA
single-stranded DNA
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the helicase separates double-stranded RNA or DNA with a 5'-3' polarity, using the energy of ATP hydrolysis. GST-tagged nsp13 shows much more efficient nucleic acid unwinding than the H6-tagged counterpart. At 0.1 second, more than 50% of the ATP is hydrolyzed hydrolysed by GST-nsp13 compared to less than 5% ATP hydrolysis by H6-nsp13
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dTTP + H2O
dTDP + phosphate
dUTP + H2O
dUDP + phosphate
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-
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GTP + H2O
GDP + phosphate
partial duplex of M13 single-stranded DNA, 50-mer, 3'-tailed
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UTP + H2O
UDP + phosphate
additional information
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ATP + H2O
ADP + phosphate
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-
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ATP + H2O
ADP + phosphate
PcrA shows 3' to 5' as well as 5' to 3' helicase activities, with substrates containing a duplex region and a 3' or 5' ss poly(dT) tail. PcrA also efficiently unwinds oligonucleotides containing a duplex region and a 5' or 3' ss tail with the potential to form a secondary structure
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ATP + H2O
ADP + phosphate
Q81JI8
strong 5' to 3' DNA helicase activity. At both 0.1 and 0.5 mM, dATP produces comparable or slightly higher levels of unwinding than ATP
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the SF1A helicase shows direct DNA binding by conserved aromatic (Trp or Phe) and electropositive (Arg) residues within the ARLs via stacking with ssDNA bases and gripping the phosphodiester backbone, respectively
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ATP + H2O
ADP + phosphate
best substrate
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ATP + H2O
ADP + phosphate
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-
?
ATP + H2O
ADP + phosphate
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-
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?
ATP + H2O
ADP + phosphate
-
Dhel I moves 5' to 3' on the DNA strand to which it is bound. Unwinding activity decreases with increasing length of the double-stranded region suggesting a distributive mode of action. ATP and dATP are the only nucleoside-5'-triphosphates that support the strand displacement reaction. Both have an optimal concentration range between 1 and 2 mM
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ATP + H2O
ADP + phosphate
Fromanvirus D29
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ATP + H2O
ADP + phosphate
Fromanvirus D29
enzyme WCGp80 is an ATP-dependent 5'->3' helicase showing low activity with the 5' 23-nt ssDNA tailed fork
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ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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-
-
?
ATP + H2O
ADP + phosphate
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-
-
-
?
ATP + H2O
ADP + phosphate
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-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
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-
-
?
ATP + H2O
ADP + phosphate
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-
-
?
ATP + H2O
ADP + phosphate
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-
-
?
ATP + H2O
ADP + phosphate
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-
-
?
ATP + H2O
ADP + phosphate
TWINKLE is the helicase at the mitochondrial DNA replication fork
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?
ATP + H2O
ADP + phosphate
DNA unwinding in 5' to 3' direction
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ATP + H2O
ADP + phosphate
hPifHD (core helicase domain) only unwinds the substrate with a 5' single-stranded DNA (ssDNA) overhang and is a 5' to 3' helicase. Pif1 specifically recognizes and unwinds DNA structures resembling putative stalled replication forks. Notably, the enzyme requires both arms of the replication fork-like structure to initiate efficient unwinding of the putative leading replication strand of such substrates. This DNA structure-specific mode of initiation of unwinding is intrinsic to the conserved core helicase domain (hPifHD) that also possesses a strand annealing activity
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ATP + H2O
ADP + phosphate
TWINKLE is a DNA helicase with 5' to 3' directionality. The enzyme needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. UTP efficiently supports DNA unwinding. ATP, GTP, and dTTP are less effective
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ATP + H2O
ADP + phosphate
enzyme ChlR1 fails to unwind the triplex substrate in the absence of ATP or in the presence of ADP or ATPgammaS
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ATP + H2O
ADP + phosphate
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5'-3' unwinding activity, enzymatic functions of the two subunit helicase-primase complex (enzyme complex consisting of UL5 and UL52 gene functions): DNA-dependent ATPase, DNA primase, and DNA helicase activities
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ATP + H2O
ADP + phosphate
the recombinant protein has both RNA and DNA duplex-unwinding activities with 5'-to-3' polarity. The DNA helicase activity of the enzyme preferentially unwinds 5'-oligopyrimidine-tailed, partial-duplex substrates and requires a tail length of at least 10 nucleotides for effective unwinding
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
PfRuvB1 is an ATPase and this activity increases significantly in the presence of ssDNA, PfRuvB1 also contains DNA helicase activity and translocates preferentially in 5' to 3' direction, substrates are M13 mp19 ssDNA and oligonucleotides
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ATP + H2O
ADP + phosphate
DNA helicase activity in 5' to 3' direction
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ATP + H2O
ADP + phosphate
DNA helicase activity in 5' to 3' direction
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?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
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ATP + H2O
ADP + phosphate
5' to 3' DNA helicase. The ATPase/helicase activity of Rrm3p is required for its role in telomeric and subtelomeric DNA replication. Because Rrm3p is telomere-associated in vivo, it likely has a direct role in telomere replication
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ATP + H2O
ADP + phosphate
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ATP hydrolysis is required for unwinding of DNA catalyzed by the DNA helicase, the enzyme moves in the 5 to 3 direction on a single-stranded DNA to catalyze unwinding of double-stranded regions of DNA in the 3' to 5' direction
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ATP + H2O
ADP + phosphate
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hydrolyzes ATP and dATP with equal efficiency. ATPase activity of the enzyme is absolutely DNA-dependent. DNA sequences containing pyrimidine stretches are more effective activators than those containing purine stretches. poly(dC) appears to be the most effective activator of the ATPase activity. DNA helicase migrates on a DNA template in 5' to 3' direction
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ATP + H2O
ADP + phosphate
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unwinds partial duplex DNA substrates, as long as 343 base pairs in length, in a reaction that is dependent on either ATP or dATP hydrolysis. The direction of the unwinding reaction is 5' to 3' with respect to the strand of DNA on which the enzyme is bound
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
5' to 3' DNA helicase. ATPase/helicase activity of Pfh1p is essential. Maintenance of telomeric DNA is not the sole essential function of Pfh1p. Although mutant spores depleted for Pfh1p proceed through S phase, they arrest with a terminal cellular phenotype consistent with a postinitiation defect in DNA replication. Telomeric DNA is modestly shortened in the absence of Pfh1p
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ATP + H2O
ADP + phosphate
5' to 3' DNA helicase
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ATP + H2O
ADP + phosphate
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the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive
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ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
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ATP + H2O
ADP + phosphate
the enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates
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ATP + H2O
ADP + phosphate
PcrA is a chromosomally encoded DNA helicase of gram-positive bacteria involved in replication of rolling circle replicating plasmids
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ATP + H2O
ADP + phosphate
hydrolyzes both ATP and dATP at similar levels. The enzyme shows 5' to 3' and 3' to 5' DNA helicase activities and binds efficiently to partially duplex DNA containing a hairpin structure adjacent to a 6-nucleotide 5' or 3' single-stranded tail and one unpaired (flap) nucleotide in the complementary strand
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ATP + H2O
ADP + phosphate
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can unwind a bubble substrate consistent with a role in nucleotide excision repair
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?
ATP + H2O
ADP + phosphate
-
the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination
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?
ATP + H2O
ADP + phosphate
ATP-dependent 5'3' DNA helicases, DNA-dependent ATPase
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?
ATP + H2O
ADP + phosphate
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DNA substrates with overhangs of 0, 6 or 9 nucleotides are unwound at similar rates and remain only partially unwound at the end of the reaction. Overhangs of 12, 15 or 20 nucleotides are unwound progressively more quickly and to completion. XPD can overcome single backbone or base modifications in both the translocated and the displaced strand. It can unwind DNA containing the bulky extrahelical adduct fluorescein and a cyclopyrimidine dimer
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ATP + H2O
ADP + phosphate
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the helicases is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding
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?
ATP + H2O
ADP + phosphate
-
the archaeal Rad50-Mre11 complex might act in association with a 5' to 3' exonuclease (NurA) and a bipolar DNA helicase indicating a probable involvement in the initiation step of homologous recombination
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?
ATP + H2O
ADP + phosphate
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the helicases is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding
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?
ATP + H2O
ADP + phosphate
ATP-dependent 5'3' DNA helicases, DNA-dependent ATPase
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?
ATP + H2O
ADP + phosphate
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
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ATP + H2O
ADP + phosphate
-
the Hjm protein is essential for cell viability. The StoHjc protein regulates the helicase activity of StoHjm by inducing conformation change of the enzyme. Hjm/Hjc mediated resolution of stalled replication forks is of crucial importance in archaea. A tentative pathway with which Hjm/Hjc interaction could have occurred at stalled replication forks is discussed
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ATP + H2O
ADP + phosphate
5' to 3' helicase activity
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?
ATP + H2O
ADP + phosphate
-
StoHjm has two main modules, the N-terminal ATPase and DNA binding module (1431) and the C-terminal helicase regulation module (414704). While the N-terminal module is active alone to hydrolyze ATP and to bind different types of DNA substrates, it does not show any helicase activity. DNA unwinding by the StoHjm protein requires the presence of domain III and IV of the C-terminal module in addition to the N-terminal module
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ATP + H2O
ADP + phosphate
the enzyme unwinds DNA in both 3'-to-5' and 5'-to-3' directions. The enzyme exhibits structure-specific single-stranded-DNA-annealing and fork regression activities in vitro
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ATP + H2O
ADP + phosphate
the enzyme unwinds Holliday junction, splayed-armDNA, aswell as 5'- or 3'-overhang with high efficiency
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?
ATP + H2O
ADP + phosphate
the enzyme unwinds Holliday junction, splayed-armDNA, aswell as 5'- or 3'-overhang with high efficiency
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?
ATP + H2O
ADP + phosphate
5' to 3' helicase activity
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?
ATP + H2O
ADP + phosphate
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
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?
ATP + H2O
ADP + phosphate
the enzyme unwinds DNA in both 3'-to-5' and 5'-to-3' directions. The enzyme exhibits structure-specific single-stranded-DNA-annealing and fork regression activities in vitro
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ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
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?
ATP + H2O
ADP + phosphate
-
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?
ATP + H2O
ADP + phosphate
utilizes the energy from ATP hydrolysis to unwind DNA with 5' to 3' polarity
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?
ATP + H2O
ADP + phosphate
-
utilizes the energy from ATP hydrolysis to unwind DNA with 5' to 3' polarity
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?
CTP + H2O
CDP + phosphate
-
-
-
?
CTP + H2O
CDP + phosphate
-
the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive
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CTP + H2O
CDP + phosphate
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-
?
dATP + H2O
dADP + phosphate
Q81JI8
strong 5' to 3' DNA helicase activity. At both 0.1 and 0.5 mM, dATP produces comparable or slightly higher levels of unwinding than ATP
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-
?
dATP + H2O
dADP + phosphate
high activity
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?
dATP + H2O
dADP + phosphate
-
Dhel I moves 5' to 3' on the DNA strand to which it is bound. Unwinding activity decreases with increasing length of the double-stranded region suggesting a distributive mode of action. ATP and dATP are the only nucleoside-5'-triphosphates that support the strand displacement reaction. Both have an optimal concentration range between 1 and 2 mM
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dATP + H2O
dADP + phosphate
-
ATP hydrolysis is required for unwinding of DNA catalyzed by the DNA helicase, the enzyme moves in the 5 to 3 direction on a single-stranded DNA to catalyze unwinding of double-stranded regions of DNA in the 3' to 5' direction. dATP shows 95% of the activity with ATP
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dATP + H2O
dADP + phosphate
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hydrolyzes ATP and dATP with equal efficiency. ATPase activity of the enzyme is absolutely DNA-dependent
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?
dATP + H2O
dADP + phosphate
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unwinds partial duplex DNA substrates, as long as 343 base pairs in length, in a reaction that is dependent on either ATP or dATP hydrolysis. The direction of the unwinding reaction is 5' to 3' with respect to the strand of DNA on which the enzyme is bound
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dATP + H2O
dADP + phosphate
-
the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive
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?
dATP + H2O
dADP + phosphate
the enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates
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dATP + H2O
dADP + phosphate
hydrolyzes both ATP and dATP at similar levels. The enzyme shows 5' to 3' and 3' to 5' helicase activities and binds efficiently to partially duplex DNA containing a hairpin structure adjacent to a 6-nucleotide 5' or 3' single-stranded tail and one unpaired (flap) nucleotide in the complementary strand
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dCTP + H2O
dCDP + phosphate
-
-
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?
dCTP + H2O
dCDP + phosphate
-
the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive
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dCTP + H2O
dCDP + phosphate
the enzyme exhibited a preference for ATP, dATP, and dCTP over the other NTP/dNTP substrates
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dGTP + H2O
dGDP + phosphate
-
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?
dGTP + H2O
dGDP + phosphate
-
the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive
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dGTP + H2O
dGDP + phosphate
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?
DNA
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the DNA strand separation is 5'-3' along one strand of double-stranded DNA. The 3'-tail is required for enzyme unwinding process, no matter whether it is single-stranded or double-stranded. When the enzyme cannot continue unwinding because of the high GC content in DNA sequence, it dissociates from the single-stranded DNA or slips back to the initial position very quickly because of the annealing stress
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DNA
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Tequatrovirus T4
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the enzyme is a DNA-dependent ATPase and a DNA helicase. DNA in a single-stranded form is strongly preferred. The enzyme can unwind extensive stretches of double-stranded DNA very rapidly, appearing to move with a 5'-3' polarity relative to the single DNA strand to which it initially binds. The protein hydrolyzes ATP and dATP to their respective nucleoside diphosphates in the presence of DNA. Other nucleotides are not detectably hydrolyzed
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?
dTTP + H2O
dTDP + phosphate
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-
-
?
dTTP + H2O
dTDP + phosphate
TWINKLE is a DNA helicase with 5' to 3' directionality. The enzyme needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. UTP efficiently supports DNA unwinding. ATP, GTP, and dTTP are less effective
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?
duplex DNA
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the dnaB protein unwinds the DNA in a reaction that requires hydrolysis of a ribonucleoside triphosphate. The dnaB protein moves 5' to 3' along the strand to which it is bound. A preformed fork is required for the protein to invade and unwind duplex DNA
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?
duplex DNA
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partially duplex DNA substrate in which a 36-mer oligonucleotide and a 25-mer oligonucleotide are annealed at, respectively, the 5'and 3' ends of linear, single-stranded M13 DNA
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?
GTP + H2O
GDP + phosphate
-
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-
?
GTP + H2O
GDP + phosphate
TWINKLE is a DNA helicase with 5' to 3' directionality. The enzyme needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. UTP efficiently supports DNA unwinding. ATP, GTP, and dTTP are less effective
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-
?
GTP + H2O
GDP + phosphate
-
the enzyme translocates in a 5'-to-3' direction with respect to the substrate strand to which it is bound. The enzyme favours adenosine nucleotides (ATP and dATP) as its energy source, but utilizes to limited extents GTP, CTP, dGTP and dCTP. ATP and dATP support unwinding activity with equal efficiency. GTP, dGTP, CTP, dCTP support unwinding activity to limited extents (5-12% of that with ATP at 1.5 mM). The ATPase activity of DNA helicase II increases proportionally with increasing lengths of single-stranded DNA cofactor. In the presence of circular DNA, ATP hydrolysis continues to increase up to the longest time tested (3 h), whereas it ceases to increase after 5-10 min in the presence of shorter oligonucleotides. The initial rate of ATP hydrolysis during the first 5 min of incubation time is not affected by DNA species used. The enzyme does not dissociate from the single-stranded DNA once it is bound and is therefore highly processive
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?
GTP + H2O
GDP + phosphate
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-
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?
partial duplex DNA
?
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the enzyme shows strong 5 to 3 helicase and ATPase activity and can also use UTP, CTP, GTP and dATP as energy source, Ca2+ as a co-factor and untailed substrate for the helicase activity. When dCTP, dGTP, dTTP, ADP or ATPgammaS are included in the reaction mixture instead of ATP, no helicase activity is detected
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?
partial duplex DNA
?
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the enzyme shows strong 5 to 3 helicase and ATPase activity and can also use UTP, CTP, GTP and dATP as energy source, Ca2+ as a co-factor and untailed substrate for the helicase activity. When dCTP, dGTP, dTTP, ADP or ATPgammaS are included in the reaction mixture instead of ATP, no helicase activity is detected
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-
?
UTP + H2O
UDP + phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
-
?
UTP + H2O
UDP + phosphate
-
-
-
?
UTP + H2O
UDP + phosphate
TWINKLE is a DNA helicase with 5' to 3' directionality. The enzyme needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. UTP efficiently supports DNA unwinding. ATP, GTP, and dTTP are less effective
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?
UTP + H2O
UDP + phosphate
-
-
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?
additional information
?
-
the enzyme has both DNA primase and DNA helicase activities. The helicase utilizes ATP hydrolysis to separate the DNA double helix into individual strands. DNA primase catalyzes the formation of short RNA oligonucleotides used as primers to begin DNA synthesis
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?
additional information
?
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the enzyme has both DNA primase and DNA helicase activities. The helicase utilizes ATP hydrolysis to separate the DNA double helix into individual strands. DNA primase catalyzes the formation of short RNA oligonucleotides used as primers to begin DNA synthesis
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?
additional information
?
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the enzyme binds to single-stranded DNA but has little or no affinity for double-stranded DNA or single-stranded RNA. The enzyme translocates in the 5'-3' direction along the strand to which it is bound and preferentially unwinds DNA substrates with a forklike structure. The enzyme also has DNA-dependent ATPase activity which has a relatively low Km for ATP (0.04 mM)
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additional information
?
-
the enzyme shows 5`-3` translocation directionality
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-
additional information
?
-
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the enzyme shows 5`-3` translocation directionality
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-
-
additional information
?
-
the enzyme shows 5`-3` translocation directionality
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-
additional information
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heterologously expressed recombinant Twm1 possesses nucleoside triphosphatase (NTPase), helicase and primase activity in vitro. Twm1 functions as a 5'->3' helicase which requires open fork-like DNA substrates. Nucleotide phosphate substrate specificity, overview. NTPase activity of Twm1 is also measured in the presence of linear dsDNA (FHA0), circular ssDNA (M13mp18) or linear ssDNA (FHA3.1)
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additional information
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heterologously expressed recombinant Twm1 possesses nucleoside triphosphatase (NTPase), helicase and primase activity in vitro. Twm1 functions as a 5'->3' helicase which requires open fork-like DNA substrates. Nucleotide phosphate substrate specificity, overview. NTPase activity of Twm1 is also measured in the presence of linear dsDNA (FHA0), circular ssDNA (M13mp18) or linear ssDNA (FHA3.1)
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additional information
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the helicase unwinds DNA 5' to 3'and has a preference for purine triphosphates as cofactors for the unwinding reaction (GTP/dGTP are better substrates than ATP/dATP. CTP/dCTP support the reaction at higher concentrations, while UTP and dTTP can hardly be utilised at all)
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additional information
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the enzyme is loaded onto a single strand of DNA at origins of replication from its complex with its loading partner DnaC, then translocates in the 5 to 3 direction, unwinding duplex DNA in an NTP-driven process
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additional information
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Fromanvirus D29
enzyme WCGp80 unwinds DNA in a 5'-3' direction at replication forks in an ATP-dependent manner. DnaB helicases prefer forks as substrates
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additional information
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Fromanvirus D29
no activity with AMP-PNP
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additional information
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the unwinding of parental duplex DNA is carried out by the replicative DNA helicase DnaB that couples NTP hydrolysis to 5'-to-3' translocation. The helicase can translocate on both single-stranded DNA and double-stranded DNA
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additional information
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HDHB interacts with the N-terminal domain of replication protein A 70-kDa subunit
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additional information
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the loading of TWINKLE onto a circular ssDNA in vitro is examined. TWINKLE is able to load onto circular ssDNA without the help of a loading factor and can support initiation of DNA replication on a closed circular dsDNA substrate in combination with only mitochondrial DNA polymerase gamma
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additional information
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efficiency of unwinding is enhanced in the presence of a heterologous single strand-binding protein or a single-stranded (ss) DNA that is complementary to the unwound strand. TWINKLE has an antagonistic activity of annealing two complementary ssDNAs that interferes with unwinding in the absence of gp2.5 single strand-binding protein or ssDNA trap. Only ssDNA and not dsDNA competitively inhibits the annealing activity, although both DNAs bind with high affinities
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additional information
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ChlR1 robustly unwinds DNA triplex substrates in an ATP-dependent manner requiring an 5'-ssDNA tail, ChlR1 can unwind an intramolecular triplex structure
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additional information
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ChlR1 robustly unwinds DNA triplex substrates in an ATP-dependent manner requiring an 5'-ssDNA tail, ChlR1 can unwind an intramolecular triplex structure
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additional information
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the purified recombinant ChlR1 protein is a DNA-dependent ATPase and unwinds partial duplex DNA substrates with a preferred 5' to 3' directionality, triplex DNA is the preferred DNA substrate for ChlR1, analysis of diverse DNA substrates, overview
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additional information
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the purified recombinant ChlR1 protein is a DNA-dependent ATPase and unwinds partial duplex DNA substrates with a preferred 5' to 3' directionality, triplex DNA is the preferred DNA substrate for ChlR1, analysis of diverse DNA substrates, overview
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additional information
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DDX11 is endowed with DNA-dependent ATPase and DNA helicase activities. DDX11 translocates on single-stranded DNA with a 5' to 3' directionality requiring ATP or, to a lesser extent, dATP to fuel this activity. DDX11 DNA strand separation requires a 5'-single-stranded region for helicase loading, since blunt-ended duplex structures do not support DNA unwinding. DDX11 helicase reaction requirements and DNA substrate specificity, overview. DDX11 preferentially unwinds forked duplex DNA substrates with non-complementary 5'- and 3'-single-stranded arms. A 3'-tail having a length between 5- and 10-nt and a 5'-tail of at least 15-nt are required for the helicase to optimally melt double-stranded DNA, duplexes having blunt ends or only a 3'-tail are not unwound. Human DDX11 directly interacts with the Ctf18-replication factor C (RFC) complex, the proliferating cell nuclear antigen (PCNA) factor, and the flap endonuclease 1 (FEN-1)
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additional information
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DDX11 is endowed with DNA-dependent ATPase and DNA helicase activities. DDX11 translocates on single-stranded DNA with a 5' to 3' directionality requiring ATP or, to a lesser extent, dATP to fuel this activity. DDX11 DNA strand separation requires a 5'-single-stranded region for helicase loading, since blunt-ended duplex structures do not support DNA unwinding. DDX11 helicase reaction requirements and DNA substrate specificity, overview. DDX11 preferentially unwinds forked duplex DNA substrates with non-complementary 5'- and 3'-single-stranded arms. A 3'-tail having a length between 5- and 10-nt and a 5'-tail of at least 15-nt are required for the helicase to optimally melt double-stranded DNA, duplexes having blunt ends or only a 3'-tail are not unwound. Human DDX11 directly interacts with the Ctf18-replication factor C (RFC) complex, the proliferating cell nuclear antigen (PCNA) factor, and the flap endonuclease 1 (FEN-1)
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additional information
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enzyme HDHB interacts directly with two initiation factors TopBP1 and Cdc45 in vitro
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additional information
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enzyme HDHB interacts directly with two initiation factors TopBP1 and Cdc45 in vitro
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additional information
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purified recombinant human DDX11 protein possesses ATPase-dependent DNA unwinding activity in vitro. Comprehensive analysis of the DDX11 helicase reaction requirements and DNA substrate specificity, overview
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additional information
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purified recombinant human DDX11 protein possesses ATPase-dependent DNA unwinding activity in vitro. Comprehensive analysis of the DDX11 helicase reaction requirements and DNA substrate specificity, overview
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additional information
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three catalytic activities are ascribed to the recombinant human mtDNA helicase: DNA-dependent NTPase, 5'-3' dsDNA unwinding, and nucleotide-independent ssDNA annealing. DNA primase activity associated with the N-terminal half of the T7 gp4 primase-helicase has not been found. DNA unwinding assay on oligonucleotide substrates, the DNA-dependent ATPase assay, several DNA binding assays and the replisome assay are employed
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additional information
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three catalytic activities are ascribed to the recombinant human mtDNA helicase: DNA-dependent NTPase, 5'-3' dsDNA unwinding, and nucleotide-independent ssDNA annealing. DNA primase activity associated with the N-terminal half of the T7 gp4 primase-helicase has not been found. DNA unwinding assay on oligonucleotide substrates, the DNA-dependent ATPase assay, several DNA binding assays and the replisome assay are employed
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additional information
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TWINKLE uses DNA annealing function to actively catalyze strand-exchange reaction between the unwinding substrate and a homologous single-stranded DNA. The mechanism of strand-exchange involves active coupling of unwinding and annealing reactions by the TWINKLE. Unlike strand-annealing, the strand-exchange reaction requires nucleotide hydrolysis and is greatly stimulated by short region of homology between the recombining DNA strands that promote joint molecule formation to initiate strand-exchange. ssDNA and dsDNA oligodeoxynucleotides of different sizes are used as helicase substrates for unwinding and strand-exchange reaction assay, substrate specificity for unwinding, strand-exchange, and branch migration with UTP as cosubstrate, detailed overview. Complementarity between the recombining strands is crucial for TWINKLE catalyzed strand-exchange reaction. TWINKLE is catalyzing the reactions of strand-exchange and joint molecule formation by using its DNA unwinding and annealing activities. TWINKLE translocates on the 5'-strand of the fork DNA to catalyze the strand-exchange reaction, and it catalyzes homologous branch migration reaction
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additional information
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TWINKLE uses DNA annealing function to actively catalyze strand-exchange reaction between the unwinding substrate and a homologous single-stranded DNA. The mechanism of strand-exchange involves active coupling of unwinding and annealing reactions by the TWINKLE. Unlike strand-annealing, the strand-exchange reaction requires nucleotide hydrolysis and is greatly stimulated by short region of homology between the recombining DNA strands that promote joint molecule formation to initiate strand-exchange. ssDNA and dsDNA oligodeoxynucleotides of different sizes are used as helicase substrates for unwinding and strand-exchange reaction assay, substrate specificity for unwinding, strand-exchange, and branch migration with UTP as cosubstrate, detailed overview. Complementarity between the recombining strands is crucial for TWINKLE catalyzed strand-exchange reaction. TWINKLE is catalyzing the reactions of strand-exchange and joint molecule formation by using its DNA unwinding and annealing activities. TWINKLE translocates on the 5'-strand of the fork DNA to catalyze the strand-exchange reaction, and it catalyzes homologous branch migration reaction
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additional information
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although the enzyme behaves as a traditional 5' to 3' helicase on conventional forked duplex substrates, fuelled by the hydrolysis of nucleoside triphosphate, it efficiently dissociates D-loop DNA substrates irrespective of whether it possesses a 5' or 3' single-stranded tailed invading strand. In contrast, the enzyme branch-migrates an open-ended mobile three-stranded DNA structure with a strong 5' to 3' directionality preference. The enzyme can load onto single-stranded DNA circles or double-stranded DNA bubble structures, and it binds both single-stranded and double-stranded DNA
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additional information
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in vitro, the enzyme stimulates Rad51-mediated heteroduplex extension in 5'-3' direction
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additional information
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in vitro, the enzyme stimulates Rad51-mediated heteroduplex extension in 5'-3' direction
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additional information
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the enzyme catalyzes duplex unwinding in the 5'-3' direction
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additional information
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the enzyme uses ATP to fuel duplex unwinding
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additional information
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TWINKLE is the helicase at the mitochondrial DNA replication fork with 5' to 3' directionality and distinct substrate requirements. The protein needs a stretch of 10 nucleotides of single-stranded DNA on the 5'-side of the duplex to unwind duplex DNA. In addition, helicase activity is not observed unless a short single-stranded 3'-tail is present. The helicase activity has an absolute requirement for hydrolysis of a nucleoside 5'-triphosphate, with UTP being the optimal substrate
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additional information
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the enzyme DnaB exhibits strong 5' to 3' helicase and ATPase activities
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additional information
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the enzyme has both helicase activity (5' to 3' DNA unwinding activity) and single-stranded DNA-dependent ATPase activity. ATP and dATP are preferred over the other NTPs and dNTPs. No helicase activity is detected when nonhydrolyzable ADP is added
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additional information
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the enzyme has both helicase activity (5' to 3' DNA unwinding activity) and single-stranded DNA-dependent ATPase activity. ATP and dATP are preferred over the other NTPs and dNTPs. No helicase activity is detected when nonhydrolyzable ADP is added
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additional information
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enzyme RuvB1 is an active DNA helicase and translocates in the 5'-3' direction
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additional information
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enzyme RuvB1 is an active DNA helicase and translocates in the 5'-3' direction
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additional information
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the enzyme is an ATPase both in the presence and absence of DNA, and this activity increases significantly in the presence of single-stranded DNA. The enzyme also contains DNA helicase activity and translocates preferentially in 5' to 3' direction
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additional information
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Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 affects telomerase activity by a different mechanism than Pif1. Pif1 helicase activity is stimulated by RNA-DNA hybrids
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additional information
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Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 affects telomerase activity by a different mechanism than Pif1. Pif1 helicase activity is stimulated by RNA-DNA hybrids
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additional information
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enzyme Rrm3p is an ATPase and 5' to 3' DNA helicase
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additional information
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Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 affects telomerase activity by a different mechanism than Pif1. Pif1 helicase activity is stimulated by RNA-DNA hybrids
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additional information
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non-hydrolysable ATP analogues do not support helicase activity. DNA helicase II lacks any detectable RNA-unwinding activity
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additional information
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various oligonucleotides and G4 polymorphic DNA structures are used as substrates. G4 structures are stabilized by the presence of cations, such as Na+ and K+, and the stability and the structure formed can differ depending on the cation species, the ionic strength and the sequence of the oligonucleotide. Determination of G4 consensus motifs from Schizosaccharomyces pombe rDNA and telomeric regions, substrate specificity, detailed overview. nPfh1 unwinds Schizosaccharoyces pombe rDNA and telomeric G4 DNA in vitro, and unwinds Phen-DC3-stabilized G4 structures. The ATP hydrolysis for the telomeric oligonucleotide is lower than for the rDNA oligonucleotide
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additional information
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various oligonucleotides and G4 polymorphic DNA structures are used as substrates. G4 structures are stabilized by the presence of cations, such as Na+ and K+, and the stability and the structure formed can differ depending on the cation species, the ionic strength and the sequence of the oligonucleotide. Determination of G4 consensus motifs from Schizosaccharomyces pombe rDNA and telomeric regions, substrate specificity, detailed overview. nPfh1 unwinds Schizosaccharoyces pombe rDNA and telomeric G4 DNA in vitro, and unwinds Phen-DC3-stabilized G4 structures. The ATP hydrolysis for the telomeric oligonucleotide is lower than for the rDNA oligonucleotide
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additional information
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various oligonucleotides and G4 polymorphic DNA structures are used as substrates. G4 structures are stabilized by the presence of cations, such as Na+ and K+, and the stability and the structure formed can differ depending on the cation species, the ionic strength and the sequence of the oligonucleotide. Determination of G4 consensus motifs from Schizosaccharomyces pombe rDNA and telomeric regions, substrate specificity, detailed overview. nPfh1 unwinds Schizosaccharoyces pombe rDNA and telomeric G4 DNA in vitro, and unwinds Phen-DC3-stabilized G4 structures. The ATP hydrolysis for the telomeric oligonucleotide is lower than for the rDNA oligonucleotide
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additional information
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the enzyme is inefficient in in vitro replication of pT181, and perhaps as a consequence, this plasmid can not be established in Streptococcus pneumoniae
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additional information
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the enzyme is inefficient in in vitro replication of pT181, and perhaps as a consequence, this plasmid can not be established in Streptococcus pneumoniae
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additional information
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helicase HerA also has ATPase activity
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additional information
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helicase HerA also has ATPase activity
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additional information
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the ATPase activity of Tk-Upf1 is determined using the single-stranded DNA (ssDNA) N-DNA70. When a 5' or 3' overhung mis-annealed primer is included as a competitive primer along with specific primers, noise DNAs derived from the misannealed primer are eliminated in the presence of Tk-Upf1. Among various double-stranded DNA (dsDNA) substrates (forked, 5' overhung, 3' overhung, and blunt-ended duplex), Tk-Upf1 has the highest unwinding activity toward 5' overhung DNAs. Noise DNAs are also eliminated in the presence of Tk-Upf1. Tk-Upf1 fully unwinds forked DNA, and has highest activity toward 5'-overhung DNA. Low activity with 3' overhung and blunt-ended duplex DNA, effect of Tk-Upf1 on PCR specificity. The enzyme unwinds mis-annealed primer/ template duplexes from the 5'-terminus during the annealing step of PCR, whereas primers perfectly bound to the target region are slightly peeled off by Tk-Upf1
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additional information
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the ATPase activity of Tk-Upf1 is determined using the single-stranded DNA (ssDNA) N-DNA70. When a 5' or 3' overhung mis-annealed primer is included as a competitive primer along with specific primers, noise DNAs derived from the misannealed primer are eliminated in the presence of Tk-Upf1. Among various double-stranded DNA (dsDNA) substrates (forked, 5' overhung, 3' overhung, and blunt-ended duplex), Tk-Upf1 has the highest unwinding activity toward 5' overhung DNAs. Noise DNAs are also eliminated in the presence of Tk-Upf1. Tk-Upf1 fully unwinds forked DNA, and has highest activity toward 5'-overhung DNA. Low activity with 3' overhung and blunt-ended duplex DNA, effect of Tk-Upf1 on PCR specificity. The enzyme unwinds mis-annealed primer/ template duplexes from the 5'-terminus during the annealing step of PCR, whereas primers perfectly bound to the target region are slightly peeled off by Tk-Upf1
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additional information
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the ATPase activity of Tk-Upf1 is determined using the single-stranded DNA (ssDNA) N-DNA70. When a 5' or 3' overhung mis-annealed primer is included as a competitive primer along with specific primers, noise DNAs derived from the misannealed primer are eliminated in the presence of Tk-Upf1. Among various double-stranded DNA (dsDNA) substrates (forked, 5' overhung, 3' overhung, and blunt-ended duplex), Tk-Upf1 has the highest unwinding activity toward 5' overhung DNAs. Noise DNAs are also eliminated in the presence of Tk-Upf1. Tk-Upf1 fully unwinds forked DNA, and has highest activity toward 5'-overhung DNA. Low activity with 3' overhung and blunt-ended duplex DNA, effect of Tk-Upf1 on PCR specificity. The enzyme unwinds mis-annealed primer/ template duplexes from the 5'-terminus during the annealing step of PCR, whereas primers perfectly bound to the target region are slightly peeled off by Tk-Upf1
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additional information
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the ATPase activity of Tk-Upf1 is determined using the single-stranded DNA (ssDNA) N-DNA70. When a 5' or 3' overhung mis-annealed primer is included as a competitive primer along with specific primers, noise DNAs derived from the misannealed primer are eliminated in the presence of Tk-Upf1. Among various double-stranded DNA (dsDNA) substrates (forked, 5' overhung, 3' overhung, and blunt-ended duplex), Tk-Upf1 has the highest unwinding activity toward 5' overhung DNAs. Noise DNAs are also eliminated in the presence of Tk-Upf1. Tk-Upf1 fully unwinds forked DNA, and has highest activity toward 5'-overhung DNA. Low activity with 3' overhung and blunt-ended duplex DNA, effect of Tk-Upf1 on PCR specificity. The enzyme unwinds mis-annealed primer/ template duplexes from the 5'-terminus during the annealing step of PCR, whereas primers perfectly bound to the target region are slightly peeled off by Tk-Upf1
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evolution
ChlR1 is a superfamily 2 DNA helicase that contains a conserved iron-sulfur domain. In humans exist four iron-sulfur DNA helicases, XPD, FANCJ, RTEL1, and ChlR1, that are implicated in autosomal recessive genetic diseases
evolution
Fromanvirus D29
DnaB are considered to be members of the RecA superfamily. All members of this superfamily, including DnaB, have a conserved C-terminal domain, known as the RecA core. DnaB helicases of the DnaB helicase family may have evolved from single domain RecA core proteins having helicase activities of their own, through the incorporation of additional N-terminal sequences. The helicases can be classified into six super-families of which DnaB which is the replicative helicase in Eubacteria, belongs to Superfamily 4. DnaB helicases are characteristically hexameric in structure. phylogenetic and evolutionary analysis identifies WCGp80 to be related to an ancestor of DnaB helicase family proteins
evolution
phylogenetic analysis of amino acid sequences of Twinkle homologues from several plants and other species shows that the Arabidopsis and plant homologues are closely clustered and are most similar to the bacteriophage T7 gp4 protein
evolution
superfamilies 1 and 2 (SF1 and SF2) comprise the largest number of helicase families and members are involved in a wide array of cellular functions that require manipulation of DNA or RNA structures, the helicases belong to the AAA+ ATPases. Helicase superfamilies can also be subdivided into those that translocate along DNA and unwind in a 3'-5' direction, e.g., SF1A, or a 5'-3 direction, e.g., SF1B. SF1 and SF2 helicases can be identified based on evolutionary conservation of seven sequence motifs (I, Ia, II-VI) that are required for ATP binding/hydrolysis, nucleic acid binding, and/or translocation. SF1 and SF2 helicases include a conserved core helicase domain that is comprised of two subdomains that share similarity with RecA ATPase/recombinase enzyme family
evolution
the RuvB family of protein contains two similar kinds of proteins i.e. RuvB1 and RuvB2 from yeast to human. Plasmodium falciparum contains three RuvB proteins (PfRuvB1, PfRuvB2 and PfRuvB3) instead of two. These proteins belong to the AAA+ class of proteins and are critical components of several multiprotein complexes involved in diverse cellular activities. PfRuvB1 shows considerable homology with human as well as yeast RuvB1 and contains Walker motif A and Walker motif B.
evolution
DNA helicase B is a robust 5'-3' superfamily I DNA helicase conserved among vertebrates
evolution
DNA/RNA helicases are classified into six superfamilies (SF1e6) defined by a set of conserved sequence motifs. Tk-Upf1 is a superfamily 1B type helicase
evolution
HELQ is a superfamily II DNA helicase
evolution
hPIF1 belongs to the evolutionarily conserved Pif1 family, which comprises multifunctional helicases with a unique 21 amino acid signature motif. Pfh1 is the sole Sschizosaccharomyces pombe Pif1 member
evolution
Pif1 family helicases are found in the genomes of organisms from all three kingdoms. Most eukaryotes, including Schizosaccharomyces pombe and humans, encode a single Pif1 family helicase, while Saccharomyces cerevisiae encodes two, ScPif1 and ScRrm3
evolution
Sen1p is a nuclear superfamily 1 RNA/DNA helicase
evolution
the enzyme belongs to the family of the iron-sulfur cluster containing DNA helicases, and the superfamily 2 (SF2) DNA helicases. SF2 Fe-S DNA helicases play critical functions in the maintenance of genome stability and are linked to rare genetic syndromes and cancer predisposition. An ancestral DDX11 gene might have given rise to a novel family of genes that are characterized by a common subtelomeric location and a similar C-terminal sequence. The function of DDX11 in sister chromatid cohesion establishment appears to be conserved throughout the evolution from yeast to humans
evolution
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DNA/RNA helicases are classified into six superfamilies (SF1e6) defined by a set of conserved sequence motifs. Tk-Upf1 is a superfamily 1B type helicase
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evolution
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Pif1 family helicases are found in the genomes of organisms from all three kingdoms. Most eukaryotes, including Schizosaccharomyces pombe and humans, encode a single Pif1 family helicase, while Saccharomyces cerevisiae encodes two, ScPif1 and ScRrm3
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evolution
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Pif1 family helicases are found in the genomes of organisms from all three kingdoms. Most eukaryotes, including Schizosaccharomyces pombe and humans, encode a single Pif1 family helicase, while Saccharomyces cerevisiae encodes two, ScPif1 and ScRrm3
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evolution
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hPIF1 belongs to the evolutionarily conserved Pif1 family, which comprises multifunctional helicases with a unique 21 amino acid signature motif. Pfh1 is the sole Sschizosaccharomyces pombe Pif1 member
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evolution
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DNA/RNA helicases are classified into six superfamilies (SF1e6) defined by a set of conserved sequence motifs. Tk-Upf1 is a superfamily 1B type helicase
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malfunction
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HDHB knockdown impairs recovery from replication stress
malfunction
RNAi of TbPIF1 causes a growth defect and kinetoplast DNA loss. Minicircle replication intermediates decrease during RNAi, and there is an accumulation of multiply interlocked, covalently closed minicircle dimers (fraction U)
malfunction
an NTD only construct (DELTA372-684) shows no ATPase activity. Several naturally occurring mutations in the enzyme sequence are determinated, e.g. pathogenic mutations in the linker region and CTD in that affect the functional organization
malfunction
autosomal recessive mutations of the DDX11 gene are responsible for a rare cohesinopathy, a rare genetic disorder named Warsaw breakage syndrome, showing both chromosomal breakages and chromatid cohesion defects. Depletion of either DDX11 or FEN-1 by siRNAs results in cohesion defects in human cells
malfunction
deficiency of the helicase, POLQ-like (HELQ) gene increases the risk of ovarian cancer
malfunction
depletion of the human DNA helicase B (HDHB) inhibits the initiation of DNA replication, suggesting a role of HDHB in the beginning of the DNA synthesis. Depletion of HDHB from human cells diminishes Cdc45 association with chromatin, and microinjection of purified recombinant HDHB protein with a nonfunctional Walker B motif into cells in early G1 inhibits the G1/S transition, whereas the wild type protein has no effect
malfunction
fibroblasts derived from xeroderma pigmentosum patients harboring mutations in XPD display increased sensitivity to UV-induced DNA damage due to defects in the NER pathway and this mutant phenotype can be rescued by expression of wild-type XPD. The XPD-DELTA277-286 mutant that is defective in MMS19 binding is able to complement the UV sensitivity phenotype of XPD-deficient fibroblasts. Although the expression of wild-type XPD is able to rescue the UV sensitivity defects seen in these cells, the expression of the XPD-DELTA277-286 mutant does not rescue the phenotype, suggesting that this mutant is incapable of fully supporting NER. Identification of a docking site in XPD that is required for recognition by the CIA targeting complex, which may have important implications for recognition of Fe-S proteins by the CIA targeting complex
malfunction
HDHB silencing results in reduced sister chromatid exchange, impaired homologous recombination repair, and delayed RPA late stage foci formation induced by ionizing radiation. A helicase-defective mutant HDHB fails to promote this reaction. HDHB-depleted cells have fewer sister chromatid exchange events and impaired homologous recombination repair induced by I-SceI cleavage on a chromosomal recombination reporter cassette. Ectopically expressed HDHB colocalizes with Rad51, Rad52, RPA and ssDNA. The ionizing radiation (IR)-induced RPA late-stage foci formation is reduced in HDHB-depleted cells, while Rad51 and gammaH2AX foci formation is not affected by HDHB silencing
malfunction
in the absence of functional Pfh1, unresolved G4 structures cause fork pausing and DNA damage. In the absence of Pfh1, G4 motifs associated with replication fork stalling are more likely to result in double strand breaks. A subset of G4 motifs have high Cdc20 binding indicative of replication fork pausing in Pfh1-depleted cells
malfunction
mtDNA helicase mutations are associated with structural rearrangements of the mitochondrial genome, elevation of mtDNA helicase levels increases the quantity of replication intermediates and alleviates pausing at the replication slow zones. A concomitant alteration in mtDNA copy number is not observed, but deletions specific to the segment of repeated elements in the immediate vicinity of the origin of replication, and an accumulation of species characteristic of replication fork stalling. Elevated levels of RNA that are retained in the replication intermediates are also found. Effects of elevated levels of the mtDNA helicase on the integrity and replication of the mitochondrial genome, overview
malfunction
mutations in Drosophila melanogaster mtDNA helicase analogously to mutations found in human patients result in severe mtDNA depletion in S2 cells, whereas alanine-substitutions of the amino acids that are conserved in prokaryotic RPDs have no effect on mtDNA copy number
malfunction
presence of G4 structures strongly inhibits the ATPase activity of nPfh1
malfunction
SEN1 mutants are unable to interact with RNA processing machinery Rnt1p and exhibit a flocculation phenotype. Mutations in SEN1 induce non-sexual flocculation in haploid mutant cells
malfunction
Twm1 gene antisense inhibition leads to mitochondrial dysfunction and reduced mtDNA copy number
malfunction
Tequatrovirus T4
-
enzyme deletion causes a delay in T4 DNA synthesis at early times of infection
malfunction
-
enzyme loss results in replication fork pausing at specific sites in subtelomeric DNA, such as at inactive replication origins, and at internal tracts of C1-3A/TG1-3 DNA
malfunction
enzyme silencing results in reduced sister chromatid exchange, impaired homologous recombination repair, and delayed replication protein A late-stage foci formation induced by ionizing radiation
malfunction
-
in the absence of functional Pfh1, unresolved G4 structures cause fork pausing and DNA damage. In the absence of Pfh1, G4 motifs associated with replication fork stalling are more likely to result in double strand breaks. A subset of G4 motifs have high Cdc20 binding indicative of replication fork pausing in Pfh1-depleted cells
-
malfunction
-
in the absence of functional Pfh1, unresolved G4 structures cause fork pausing and DNA damage. In the absence of Pfh1, G4 motifs associated with replication fork stalling are more likely to result in double strand breaks. A subset of G4 motifs have high Cdc20 binding indicative of replication fork pausing in Pfh1-depleted cells
-
malfunction
-
presence of G4 structures strongly inhibits the ATPase activity of nPfh1
-
metabolism
cooperative role of Rnt1p, Rrp6p and the Nrd1-Nab3-Sen1 (NNS) complex in the repression of flocculation FLO genes
metabolism
human mitochondrial (mt) DNA is replicated by a minimal T7-like replisome that consists of the nuclear-encoded DNA polymerase gamma, DNA helicase TWINKLE, and single strand DNA binding protein (mtSSB)
metabolism
pathological conditions impairing functions of mitochondria often lead to compensatory upregulation of the mitochondrial DNA (mtDNA) replisome machinery, and the replicative DNA helicase appears to be a key factor in regulating mtDNA copy number. Upregulation of mtDNA helicase promotes the process of mtDNA replication but also results in genome destabilization
metabolism
role of human DDX11 in cellular DNA metabolism and relevant protein interactions, overview. DDX11 is reported to interact with a number of different proteins involved in DNA replication, DNA damage response, sister chromatid cohesion and chromatin architecture and is thought to be a key player in all these important cellular pathways. Human DDX11 directly interacts with and stimulate the enzymatic activity of FEN-1
metabolism
Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 and Pif1 interact and their concerted activities ensure proper telomere length homeostasis in vivo. Modelling of Hrq1 and Pif1 cooperatively contributing to telomere length homeostasis in yeast, overview. Hrq1 affects telomerase activity by a different mechanism than Pif1. Pif1 acts on a long (50 nt) primer. Pif1 shows a complex activity profile over the range of concentrations tested
metabolism
several human helicases, such as WRN, FANCJ, BLM and PIF1 (hPIF1), are G4-binding helicases that are linked to genetic diseases. For example, the WRN helicase is associated with Werner syndrome, FANCJ with Fanconi anemia and hPIF1 with familial breast cancer
metabolism
the association of the xeroderma pigmentosum group D DNA helicase (XPD) with transcription factor IIH is regulated by the cytosolic iron-sulfur cluster assembly pathway, assembly of an Fe-S cluster on XPD requires the CIA targeting complex
metabolism
-
several human helicases, such as WRN, FANCJ, BLM and PIF1 (hPIF1), are G4-binding helicases that are linked to genetic diseases. For example, the WRN helicase is associated with Werner syndrome, FANCJ with Fanconi anemia and hPIF1 with familial breast cancer
-
metabolism
-
Saccharomyces cerevisiae Hrq1 and Pif1 DNA helicases synergistically modulate telomerase activity in vitro. The helicases alone have equal-but-opposite biphasic effects on telomerase, with Hrq1 stimulating activity at high concentrations. When the helicases are combined in reactions, they synergistically inhibit or stimulate telomerase activity depending on which helicase is catalytically active. Hrq1 and Pif1 interact and their concerted activities ensure proper telomere length homeostasis in vivo. Modelling of Hrq1 and Pif1 cooperatively contributing to telomere length homeostasis in yeast, overview. Hrq1 affects telomerase activity by a different mechanism than Pif1. Pif1 acts on a long (50 nt) primer. Pif1 shows a complex activity profile over the range of concentrations tested
-
physiological function
-
cellular exposure to UV irradiation, camptothecin, or hydroxyurea induces accumulation of HDHB on chromatin in a dose- and time-dependent manner, preferentially in S phase cells. Replication stress-induces recruitment of HDHB to chromatin is independent of checkpoint signaling but correlates with the level of replication protein A recruited to chromatin
physiological function
-
in Sulfolobus acidocaldarius, the Mre11 protein and the RadA recombinase might play an active role in the repair of DNA damage introduced by gamma rays and/or may act as DNA damage sensors. The functional interaction between Mre11, Rad50 and the HerA helicase suggest that each protein play different roles when acting on its own or in association with its partners. Interaction of the Mre11 protein with both Rad50 and the HerA bipolar helicase
physiological function
TbPIF1 functions in minicircle replication
physiological function
-
in thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during homologous recombination-dependent DNA repair
physiological function
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
physiological function
aromatic-rich loops as coupling motifs that link DNA binding and ATP hydrolysis, the conserved SF1 and SF2 helicase motifs mediate ATP binding and hydrolysis and convert the released chemical energy into the mechanical energy required for translocation and DNA unwinding
physiological function
-
helicase DnaB is important in the initiation and extension stages of DNA replication. DnaB proteins also exhibit ATPase activity, which provides the energy necessary for their helicase activity, the helicase activity of MtbDnaB has 5' to 3 polarity. The ATPase activity of DnaB is stimulated in the presence of ssDNA
physiological function
the enzyme plays a role in organelle DNA replication. The helicase utilizes ATP hydrolysis to separate the DNA double helix into individual strands. DNA primase catalyzes the formation of short RNA oligonucleotides used as primers to begin DNA synthesisesis
physiological function
Fromanvirus D29
the primary function of DNA helicases is to act as motor proteins to unwind double-stranded DNA, RNA and DNA-RNA hybrids. The energy required for this purpose is derived from the hydrolysis of NTP. DnaB helicases are characteristically hexameric in structure and unwind DNA in an unidirectional manner in the 5'-3' direction
physiological function
DDX11 plays multifaceted roles in genome stability maintenance. Potential role of human DDX11 in oncogenesis. DDX11 functions in sister chromatid cohesion, in DNA repair, and in DNA repair and replication fork stabilization, detailed overview. The helicase activity of DDX11 is shown to be capable of displacing duplex regions up to 100 base pairs, which can be extended to 500 base pairs by replication protein A (RPA) or the Ctf18-RFC complex. DDX11 is endowed with DNA-dependent ATPase and DNA helicase activities. DDX11 translocates on single-stranded DNA with a 5' to 3' directionality requiring ATP or, to a lesser extent, dATP to fuel this activity. Moreover, DDX11 DNA strand separation requires a 5'-single-stranded region for helicase loading, since blunt-ended duplex structures do not support DNA unwinding
physiological function
DNA helicase B (DHB) is a DNA-dependent ATPase, function of enzyme HDHB during DNA replication initiation, overview. HDHB interacts directly with two initiation factors TopBP1 and Cdc45, which are part of the pre-initiation complex (pre-IC). Both, the N-terminus and the helicase domain of HDHB bind to the N-terminus of Cdc45. HDHB may facilitate Cdc45 recruitment at G1/S in human cells. Cdc45 is a key factor in the DNA replication initiation process, and HDHB promotes recruitment of Cdc45 to chromatin. Enzyme HDHB relieves RPA-mediated inhibition of RNA primer synthesis by DNA polymerase alpha-primase on single-stranded DNA, a property typically associated with primosome activity that is needed for replication
physiological function
DNA helicases are essential components of the DNA replication, repair and recombination machinery across taxa. The replicative DNA helicases are members of the AAA+ family of ATPases and contain a conserved alpha-beta core structure domain that carries the conserved amino acid sequence motifs required for nucleotide hydrolysis. The ssDNA annealing activity might be involved in recombination-mediated replication, a mtDNA replication mechanism supported by physiological studies of mtDNA replication intermediates from human heart, or possibly in replication fork regression during DNA repair as has been described in prokaryotic and nuclear genomes
physiological function
DNA helicases are essential components of the DNA replication, repair and recombination machinery across taxa. The replicative DNA helicases are members of the AAA+ family of ATPases and contain a conserved alpha-beta core structure domain that carries the conserved amino acid sequence motifs required for nucleotide hydrolysis. The ssDNA annealing activity opposes the dsDNA unwinding activity of human mtDNA helicase in the absence of an SSB or a ssDNA trap, and only ssDNA but not dsDNA serves as a competitive inhibitor of annealing activity even though the helicase is shown to bind dsDNA. The ssDNA annealing activity might be involved in recombination-mediated replication, a mtDNA replication mechanism supported by physiological studies of mtDNA replication intermediates from human heart, or possibly in replication fork regression during DNA repair as has been described in prokaryotic and nuclear genomes
physiological function
DNA helicases are essential components of the DNA replication, repair and recombination machinery across taxa. The replicative DNA helicases are members of the AAA+ family of ATPases and contain a conserved alpha-beta core structure domain that carries the conserved amino acid sequence motifs required for nucleotide hydrolysis. The ssDNA annealing activity opposes the dsDNA unwinding activity of human mtDNA helicase in the absence of an SSB or a ssDNA trap, and only ssDNA but not dsDNA serves as a competitive inhibitor of annealing activity even though the helicase is shown to bind dsDNA. The ssDNA annealing activity might be involved in recombination-mediated replication, a mtDNA replication mechanism supported by physiological studies of mtDNA replication intermediates from human heart, or possibly in replication fork regression during DNA repair as has been described in prokaryotic and nuclear genomes. Importance of the enzyme for mitochondrial function and human health
physiological function
fundamental properties of DNA/RNA helicases are nucleic acid binding, ATP hydrolysis, translocation, unwinding of duplex nucleic acids, and displacement of proteins bound to the nucleic acid substrate. Among various double-stranded DNA (dsDNA) substrates (forked, 5' overhung, 3' overhung, and blunt-ended duplex), Tk-Upf1 has the highest unwinding activity toward 5' overhung DNAs. Noise DNAs are also eliminated in the presence of Tk-Upf1 at concentrations 10fold lower than those required to yield a comparable reduction with Thermococcus kodakarensis superfamily 2B type helicase Tk-EshA
physiological function
G-rich telomeric and ribosomal DNA sequences from the fission yeast genome form stable G-quadruplex DNA structures in vitro and are unwound by the Pfh1 DNA helicase, as well as G4 motifs from Schizosaccharoyces pombe rDNA and , that form predominantly inter- and intramolecular G4 structures, respectively. Mutations in the G-tracts of rDNA and telomeric G4 DNA oligonucleotides inhibit the formation of G4 structures
physiological function
human DNA helicase B (HDHB) is a robust 5'-3' DNA helicase which accumulates on chromatin in cells exposed to DNA damage. HDHB facilitates cellular recovery from replication stress, it plays a role in DNA damage response. In vitro, HDHB stimulates Rad51-mediated heteroduplex extension in 5'-3' direction. HDHB promotes homologous recombination in vivo and stimulates 5'-3' heteroduplex extension during Rad51-mediated strand exchange in vitro
physiological function
Pfh1, the Schizosaccharomyces pombe Pif1 helicase, is essential for maintenance of both the nuclear and mitochondrial genomes. Many G4 motifs in the Schizosaccharomyces pombe genome are associated with Pfh1. Pfh1-associated G4 motifs are located on the transcribed strand of highly transcribed genes significantly more often than expected, suggesting that Pfh1 has a function in replication or transcription at these sites. DNA damage occurs near G4 motifs. Pif1 family helicases unwind G4 structures robustly in vitro and suppress G4-induced DNA damage
physiological function
Saccharomyces cerevisiae Pif1 DNA helicase synergistically modulates telomerase activity. It is a catalytic inhibitor of telomerase. The enzyme is involved in telomerase regulation together with DNA helicase Hrq1
physiological function
Sen1p is a transcriptional termination factor in Saccharoymces cerevisiae. It is a nuclear superfamily 1 RNA/DNA helicase that is encoded by an essential gene SEN1. It is a key component of the NNS complex that terminates transcription of most non-coding transcripts, like small nuclear (sn) and small nucleolar (sno) RNAs, and some coding transcripts at RNA polymerase pause sites. The NNS complex interacts with the Trf4/Air2/Mtr4p polyadenylation (TRAMP) complex to mediate 30-end formation of some mRNAs, snRNAs, snoRNAs, and cryptic unstable transcripts (CUTs). Nrd1p and Sen1p function by interacting with different phosphorylated forms of the C-terminal domain (CTD). Two different mechanisms are reported for the association of Sen1p with Rpb1p: either direct binding to the Ser2-phosphorylated CTD or through indirect interaction with the Ser5-phosphorylated CTD as a component of the NNS complex. In another mechanism, exchange of Nrd1p and Pcf11p on chromatin facilitate RNA Pol II pausing and CTD Ser2 phosphorylation, promoting. Sen1p activity that is required for NNS-dependent transcription termination in vivo. Sen1p interacts with Glc7p, the yeast protein phosphatase 1 and a component of the cleavage and polyadenylation facto (CPF). Glc7p can dephosphorylate Sen1p in vitro, which might affect NNS complex functionality
physiological function
the dominant functions of HELQ are ATP-dependent helicase activity and participation in the DNA repair process. Analysis of the role of HELQ in DNA replicaxadtion, DNA repair and maintenance of genomic stability. Molecular function ontology of HELQ, overview
physiological function
the enzyme is involved in the replication of the mitochondrial genome. Replication of mtDNA requires two key mitochondrial enzymes: DNA polymerase gamma (Pol gamma) and mtDNA helicase. Upregulation of mtDNA helicase promotes the process of mtDNA replication but also results in genome destabilization
physiological function
the human mitochondrial DNA replisome is the ring-shaped helicase TWINKLE, which catalyzes branch migration by resolving homologous four-way junction DNA. Despite being a helicase, TWINKLE has unique DNA annealing activity. TWINKLE uses DNA annealing function to actively catalyze strand-exchange reaction between the unwinding substrate and a homologous single-stranded DNA. The mechanism of strand-exchange involves active coupling of unwinding and annealing reactions by the TWINKLE. TWINKLE catalyzes branch migration by resolving homologous four-way junction DNA. These four DNA modifying activities of TWINKLE: strand-separation, strand-annealing, strand-exchange, and branch migration suggesting a dual role of TWINKLE in mitochondrial DNA maintenance. In addition to playing a major role in fork progression during leading strand DNA synthesis, TWINKLE is involved in recombinational repair of the human mitochondrial DNA
physiological function
Twm1 is a replicative mitochondrial DNA helicase which is capable of priming DNA for replication. Non-metazoan Twinkle functions in the initiation of mitochondrial DNA replication. Twm1 is important for mitochondrial function as it maintains mitochondrial DNA copy number in vivo. Twm1 is a helicase which unwinds DNA resembling open forks, although it can act upon substrates with a single 3' overhang, albeit less efficiently. Furthermore, unlike human Twinkle, Twm1 has primase activity in vitro. Twinkle helicases function as 5'->3' helicases and, similar to other replicative helicases, form ring-shaped hexamers to unwind dsDNA at the replication fork
physiological function
-
efficient 5'-3' DNA end resection by the helicase HerA/nuclease NurA complex is essential for cell viability in Sulfolobus islandicus
physiological function
Tequatrovirus T4
-
the bacteriophage T4 dda protein is a 5'-3' DNA helicase that stimulates DNA replication and recombination reactions in vitro and plas a role in the initiation of T4 DNA replication in vivo
physiological function
-
the dnaB protein is the primary replicative helicase of Escherichia coli and actively and processively migrates along the lagging strand template, serving both to unwind the DNA duplex in advance of the leading strand and to potentiate synthesis by the bacterial primase of RNA primers for the nascent (Okazaki) fragments of the lagging strand
physiological function
-
the enzyme aids DNA synthesis by the mitochondrial DNA polymerase through G-quadruplexes
physiological function
the enzyme facilitates cellular recovery from replication stress. The enzyme promotes homologous recombination in vivo and stimulates 5'-3' heteroduplex extension during Rad51-mediated strand exchange in vitro
physiological function
-
the enzyme is an essential player in mitochondrial DNA replication
physiological function
-
the enzyme promotes replication fork progression through telomeric and subtelomeric DNA
physiological function
Tequatrovirus T4
-
the enzyme unwinds DNA in the 5'-to-3' direction, stimulates the rate of DNA strand displacement DNA synthesis at an in vitro replication fork, and removes DNA-binding proteins that block replication fork movement. The enzyme stimulates both DNA replication and recombination reactions. The protein is involved in the initiation of origin-dependent DNA synthesis
physiological function
-
the helicase facilitates telomere replication and has an replication protein A-dependent role during telomere lengthening. The enzyme is essential for maintenance of both nuclear and mitochondrial DNAs
physiological function
-
in thermophilic archaea, the HerA helicase and NurA nuclease cooperate with the highly conserved Mre11 and Rad50 proteins during homologous recombination-dependent DNA repair
-
physiological function
-
fundamental properties of DNA/RNA helicases are nucleic acid binding, ATP hydrolysis, translocation, unwinding of duplex nucleic acids, and displacement of proteins bound to the nucleic acid substrate. Among various double-stranded DNA (dsDNA) substrates (forked, 5' overhung, 3' overhung, and blunt-ended duplex), Tk-Upf1 has the highest unwinding activity toward 5' overhung DNAs. Noise DNAs are also eliminated in the presence of Tk-Upf1 at concentrations 10fold lower than those required to yield a comparable reduction with Thermococcus kodakarensis superfamily 2B type helicase Tk-EshA
-
physiological function
-
Pfh1, the Schizosaccharomyces pombe Pif1 helicase, is essential for maintenance of both the nuclear and mitochondrial genomes. Many G4 motifs in the Schizosaccharomyces pombe genome are associated with Pfh1. Pfh1-associated G4 motifs are located on the transcribed strand of highly transcribed genes significantly more often than expected, suggesting that Pfh1 has a function in replication or transcription at these sites. DNA damage occurs near G4 motifs. Pif1 family helicases unwind G4 structures robustly in vitro and suppress G4-induced DNA damage
-
physiological function
-
the enzyme physically interacts with StoHjc, the Holliday junction-specific endonuclease from Sulfolobus tokodaii. The unwinding activity of the helicase (StoHjm) is inhibited by StoHjc in vitro. These results may suggest that the Hjm/Hel308 family helicases, in association with Hjc endonucleases, are involved in processing of stalled replication forks
-
physiological function
-
Pfh1, the Schizosaccharomyces pombe Pif1 helicase, is essential for maintenance of both the nuclear and mitochondrial genomes. Many G4 motifs in the Schizosaccharomyces pombe genome are associated with Pfh1. Pfh1-associated G4 motifs are located on the transcribed strand of highly transcribed genes significantly more often than expected, suggesting that Pfh1 has a function in replication or transcription at these sites. DNA damage occurs near G4 motifs. Pif1 family helicases unwind G4 structures robustly in vitro and suppress G4-induced DNA damage
-
physiological function
-
G-rich telomeric and ribosomal DNA sequences from the fission yeast genome form stable G-quadruplex DNA structures in vitro and are unwound by the Pfh1 DNA helicase, as well as G4 motifs from Schizosaccharoyces pombe rDNA and , that form predominantly inter- and intramolecular G4 structures, respectively. Mutations in the G-tracts of rDNA and telomeric G4 DNA oligonucleotides inhibit the formation of G4 structures
-
physiological function
-
the helicase facilitates telomere replication and has an replication protein A-dependent role during telomere lengthening. The enzyme is essential for maintenance of both nuclear and mitochondrial DNAs
-
physiological function
-
Saccharomyces cerevisiae Pif1 DNA helicase synergistically modulates telomerase activity. It is a catalytic inhibitor of telomerase. The enzyme is involved in telomerase regulation together with DNA helicase Hrq1
-
physiological function
-
fundamental properties of DNA/RNA helicases are nucleic acid binding, ATP hydrolysis, translocation, unwinding of duplex nucleic acids, and displacement of proteins bound to the nucleic acid substrate. Among various double-stranded DNA (dsDNA) substrates (forked, 5' overhung, 3' overhung, and blunt-ended duplex), Tk-Upf1 has the highest unwinding activity toward 5' overhung DNAs. Noise DNAs are also eliminated in the presence of Tk-Upf1 at concentrations 10fold lower than those required to yield a comparable reduction with Thermococcus kodakarensis superfamily 2B type helicase Tk-EshA
-
physiological function
-
efficient 5'-3' DNA end resection by the helicase HerA/nuclease NurA complex is essential for cell viability in Sulfolobus islandicus
-
additional information
-
an MtbSSB mutant with decreased binding affinity for ssDNA can stimulate the helicase activity of MtbDnaB over a wider concentration range than wild-type MtbSSB suggesting that MtbSSB assists in the loading of MtbDnaB on the DNA replication fork
additional information
structure comparisons of SF1 and SF2 helicases, SF1 and SF2 helicase domains structures and substrate-bound SF1 and SF2 helicase structures, structure-function relationship, overview
additional information
Fromanvirus D29
the DnaB helicase activity is primarily a function of the RecA core although additional N-terminal sequences may be necessary for fine tuning its activity and stability. WCGp80, like several other DnaB helicases, possess tryptophanyl residues within the RecA core region
additional information
enzyme XPD is present in two mutually exclusive protein complexes, i.e. with TFIIH complex subunits (XPB, cyclin H, CDK7, and GTF2H1) as well as with the CIA targeting complex (MMS19, CIAO1, and FAM96B), proteomic analysis, overview. XPD assembly into TFIIH requires sufficient cellular iron and the ability to bind an Fe-S cluster cofactor. Physical association of XPD with MMS19 is required for both its incorporation into TFIIH and DNA repair
additional information
G-quadruplexes (G4s) are stable non-canonical DNA secondary structures consisting of stacked arrays of four guanines, each held together by Hoogsteen hydrogen bonds. Sequences with the ability to form these structures in vitro, G4 motifs, are found throughout bacterial and eukaryotic genomes. Genomic distribution and evolutionary conservation of G4 motifs in four fission yeast species are determined via genome-wide search for DNA sequences with the potential to form G4 structures, overview. Identification of all sequences that contain four runs of three or more guanine base pairs (bp), G-islands, separated by loop regions of no more than 25 bp (G > or = 3 N1 25)3 G > or = 3. Regions with more than four G-islands separated by < or = 25 bp are counted as a single G4 motif. Excluding repetitive DNA, the Schizosaccharomyces pombe genome contains 446 G4 motifs that match this query pattern with a density of 0.036 G4 motifs/kilobase
additional information
-
G-quadruplexes (G4s) are stable non-canonical DNA secondary structures consisting of stacked arrays of four guanines, each held together by Hoogsteen hydrogen bonds. Sequences with the ability to form these structures in vitro, G4 motifs, are found throughout bacterial and eukaryotic genomes. Genomic distribution and evolutionary conservation of G4 motifs in four fission yeast species are determined via genome-wide search for DNA sequences with the potential to form G4 structures, overview. Identification of all sequences that contain four runs of three or more guanine base pairs (bp), G-islands, separated by loop regions of no more than 25 bp (G > or = 3 N1 25)3 G > or = 3. Regions with more than four G-islands separated by < or = 25 bp are counted as a single G4 motif. Excluding repetitive DNA, the Schizosaccharomyces pombe genome contains 446 G4 motifs that match this query pattern with a density of 0.036 G4 motifs/kilobase
additional information
structure comparisons of human, mouse, and Drosophila melanogaster enzymes, modular architecture, overview. Modeling of the C-terminal domain of Drosophila melanogaster mtDNA helicase also provides a structure that resembles the homologous domain of all the DNA helicases mentioned. Modelling of the RPD domain
additional information
structure comparisons of human, mouse, and Drosophila melanogaster enzymes, modular architecture, overview. Modelling of the RPD domain
additional information
-
structure comparisons of human, mouse, and Drosophila melanogaster enzymes, modular architecture, overview. Modelling of the RPD domain
additional information
structure comparisons of human, mouse, and Drosophila melanogaster enzymes, modular architecture, overview. Structural model for the RNA polymerase-like domain (RPD) of human mtDNA helicase, overview. In the C-terminal half of the NTD of human mtDNA helicase, the RPD adopts a conformation comprising two subdomains: an N-terminal region and a TOPRIM fold
additional information
-
structure comparisons of human, mouse, and Drosophila melanogaster enzymes, modular architecture, overview. Structural model for the RNA polymerase-like domain (RPD) of human mtDNA helicase, overview. In the C-terminal half of the NTD of human mtDNA helicase, the RPD adopts a conformation comprising two subdomains: an N-terminal region and a TOPRIM fold
additional information
structure-function analysis of DNA helicase HELQ, overview. Three-dimensional ligand binding model, the ligand binding sites are distributed over Ile333, Lys335, Tyr337, Gln340, Ser362, Gly363, Gly364, Lys365, Thr366, Leu367, Lys397, and Asn678
additional information
three-dimensional homology model of DDX11 using as templates both the 10 A resolution cryo-EM structure of human XPD in the TFIIH complex (PDB ID 5IVW), as well as the high resolution crystallographic structure of archaeal XPD enzyme from Thermoplasma acidophilum (PDB ID 4A15)
additional information
-
three-dimensional homology model of DDX11 using as templates both the 10 A resolution cryo-EM structure of human XPD in the TFIIH complex (PDB ID 5IVW), as well as the high resolution crystallographic structure of archaeal XPD enzyme from Thermoplasma acidophilum (PDB ID 4A15)
additional information
-
G-quadruplexes (G4s) are stable non-canonical DNA secondary structures consisting of stacked arrays of four guanines, each held together by Hoogsteen hydrogen bonds. Sequences with the ability to form these structures in vitro, G4 motifs, are found throughout bacterial and eukaryotic genomes. Genomic distribution and evolutionary conservation of G4 motifs in four fission yeast species are determined via genome-wide search for DNA sequences with the potential to form G4 structures, overview. Identification of all sequences that contain four runs of three or more guanine base pairs (bp), G-islands, separated by loop regions of no more than 25 bp (G > or = 3 N1 25)3 G > or = 3. Regions with more than four G-islands separated by < or = 25 bp are counted as a single G4 motif. Excluding repetitive DNA, the Schizosaccharomyces pombe genome contains 446 G4 motifs that match this query pattern with a density of 0.036 G4 motifs/kilobase
-
additional information
-
G-quadruplexes (G4s) are stable non-canonical DNA secondary structures consisting of stacked arrays of four guanines, each held together by Hoogsteen hydrogen bonds. Sequences with the ability to form these structures in vitro, G4 motifs, are found throughout bacterial and eukaryotic genomes. Genomic distribution and evolutionary conservation of G4 motifs in four fission yeast species are determined via genome-wide search for DNA sequences with the potential to form G4 structures, overview. Identification of all sequences that contain four runs of three or more guanine base pairs (bp), G-islands, separated by loop regions of no more than 25 bp (G > or = 3 N1 25)3 G > or = 3. Regions with more than four G-islands separated by < or = 25 bp are counted as a single G4 motif. Excluding repetitive DNA, the Schizosaccharomyces pombe genome contains 446 G4 motifs that match this query pattern with a density of 0.036 G4 motifs/kilobase
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N596A
the mutant is defective in helicase activity (greater than four orders of magnitude compared to the wild type enzyme)
N604A
the mutant is defective in helicase activity (greater than four orders of magnitude compared to the wild type enzyme)
Y598A
the mutant is defective in helicase activity (10fold compared to the wild type enzyme)
N596A
-
the mutant is defective in helicase activity (greater than four orders of magnitude compared to the wild type enzyme)
-
N604A
-
the mutant is defective in helicase activity (greater than four orders of magnitude compared to the wild type enzyme)
-
Y598A
-
the mutant is defective in helicase activity (10fold compared to the wild type enzyme)
-
A326T
site-directed mutagenesis
A442P
site-directed mutagenesis, the catalytic mutant shows a lethal phenotype and and mtDNA depletion
I334P
site-directed mutagenesis, the catalytic mutant shows a lethal phenotype and mtDNA depletion
R341Q
site-directed mutagenesis
W441C
site-directed mutagenesis
K201A
Fromanvirus D29
site-directed mutagenesis
A318T
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) comparable to wild-type
A349P
expression of a FANCJ mutant protein with a pathogenic A349P amino acid substitution in a wild-type background exerts a dominant negative effect on resistance to DNA cross-linking agents or TMS
A475P
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows lowest kcat (ATP) value
C190S
site-directed mutagenesis
DELTAQ25
mutant bearing a deletion of Q25 shows a similar phenotype as Q25A
I367T
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) slightly decreased compared to wild-type, mutant shows a higher Km (ATP) and kcat value compared to wild-type
K319E
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) comparable to wild-type
K319T
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
K421A
-
the Walker A mutant K421A of TWINKLE fails to unwind dsDNA
K50R
site-directed mutagenesis, ATPase dead mutant, fails completely to unwind triplex substrates
K52R
mutant is seriously compromised in its ATPase activity, kcat (ATP) highly decreased compared to wild-type
K897del
site-directed mutagenesis, the mutant fails in unwinding the DNA substrates
P335L
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
Q25A
Q25A mutation of the invariant glutamine in the Q motif abolishes its ability to complement cisplatin or telomestatin sensitivity of a fancj null cell line and exerts a dominant negative effect. Mutant shows impaired FANCJ helicase activity and ATPase activity but displays ATP binding and temperature-induced unfolding transition similar to wild-type. Mutant exists only as a monomer. Km (ATP) increased compared to wild-type, kcat 10fold decreased compared to wild-type
R112H
-
most common mutations in TTD patients, amino acid substitution R112H, is localized in the Fe-S domain of XPD just before the first conserved cysteine residue. Missense mutation results in a complete loss of XPD helicase activity and a reduced basal transcription activity of the TFIIH complex
R303W
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) comparable to wild-type, mutant is much more sensitive to heat inactivation than wild-type
R334Q
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
R354P
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
R357P
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) slightly decreased compared to wild-type
R374Q
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows a higher Km (ATP) value compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) and a 2fold increase in Kd (ssDNA) value compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
S369Y
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) increased compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) value compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
T457I
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
W315L
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) slightly decreased compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
W474C
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
Y508C
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) value compared to wild-type
R227C
-
site-directed mutagenesis, mutation in the ATP binding site ARPGVGKS
G1747D
site-directed mutagenesis, the sen1-1 mutation affects function and is present in a conserved ATP-helicase region of SEN1, and this single base change results in a heat-sensitive mutation that alters the cellular abundance of many RNA species. The mutation causes an upregulation of FLO genes
K128E
site-directed mutagenesis, the mutation affects protein interactions, the mutant shows the flocculation phenotype
K260A
-
helicase-dead mutant
K264A
site-directed mutagenesis, catalytically inactive mutant, the mutant shows increased KD value, but unaltered DNA binding compared to wild-type. Pif1-K264A has no significant effects on overall telomerase activity relative to the telomerase alone control
R302W
site-directed mutagenesis, the mutation affects protein interactions, the mutant shows an unaltered phenotype compared to wild-type
K264A
-
site-directed mutagenesis, catalytically inactive mutant, the mutant shows increased KD value, but unaltered DNA binding compared to wild-type. Pif1-K264A has no significant effects on overall telomerase activity relative to the telomerase alone control
-
K337A
K337A and the K337R alleles are unable to supply the essential function of Pfh1p
K337R
K337A and the K337R alleles are unable to supply the essential function of Pfh1p
K338A
an ATPase-inactive Pfh1 variant
K388A
-
helicase dead variant
K338A
-
an ATPase-inactive Pfh1 variant
-
K388A
-
helicase dead variant
-
A349P
mutation destabilizes the Fe-S cluster and abolishes helicase activity
C105S
mutant enzyme contains no Fe-S cluster, complete loss of helicase activity
C137S
mutant enzyme contains no Fe-S cluster
C88S
mutant enzyme contains no Fe-S cluster, complete loss of helicase activity
R112H
mutation destabilizes the Fe-S cluster and abolishes helicase activity
A349P
-
mutation destabilizes the Fe-S cluster and abolishes helicase activity
-
C105S
-
mutant enzyme contains no Fe-S cluster, complete loss of helicase activity
-
C137S
-
mutant enzyme contains no Fe-S cluster
-
C88S
-
mutant enzyme contains no Fe-S cluster, complete loss of helicase activity
-
R112H
-
mutation destabilizes the Fe-S cluster and abolishes helicase activity
-
D176E
-
mutant with reduced ATPase activity compared to the wild type enzyme
D176N
-
mutant with severely reduced ATPase activity compared to the wild type enzyme
E356D
-
mutant with reduced ATPase activity compared to the wild type enzyme
E356Q
-
mutant with severely reduced ATPase activity compared to the wild type enzyme
K154R
-
the mutant has no ATPase activity
R381K
-
the mutant has no ATPase activity
D176E
-
mutant with reduced ATPase activity compared to the wild type enzyme
-
D176N
-
mutant with severely reduced ATPase activity compared to the wild type enzyme
-
E356D
-
mutant with reduced ATPase activity compared to the wild type enzyme
-
E356Q
-
mutant with severely reduced ATPase activity compared to the wild type enzyme
-
K154R
-
the mutant has no ATPase activity
-
A359T
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) value compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
A359T
naturally occurring mutation in the linker region or CTD of the human enzyme
F485L
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type, mutant shows a 3-4fold increase in Kd (dsDNA) value compared to wild-type, mutant is much more sensitive to heat inactivation than wild-type
F485L
naturally occurring mutation in the linker region or CTD of the human enzyme
L381P
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) increased compared to wild-type, mutant shows a higher Km (ATP) and kcat value compared to wild-type
L381P
naturally occurring mutation in the linker region or CTD of the human enzyme
S369P
mutation associated with mitochondrial disease does not cause profound defects in DNA binding, DNA helicase function, or ATPase activity, kcat/Km (ATP) decreased compared to wild-type
S369P
naturally occurring mutation in the linker region or CTD of the human enzyme
E355A
mutation results in loss of ATPase and DNA helicase activities, and also dsDNA-binding ability, indicating that this residue is involved in the coupling of ATP hydrolysis, dsDNA-binding, and helicase activities
E355A
-
mutation results in loss of ATPase and DNA helicase activities, and also dsDNA-binding ability, indicating that this residue is involved in the coupling of ATP hydrolysis, dsDNA-binding, and helicase activities
-
additional information
recombinant expression of antisence Twm1 construct in Dictyostelium discoideum AX2 cells leading to mitochondrial dysfunction and reduced mtDNA copy number. Ethidium bromide exposure increases twm1 expression and results in mtDNA loss from which antisense transformants are less able to recover. Generation of a truncated Twm1 with 599 amino acids and 68 kDa, lacking the first 154 and last 19 amino acids of the full length protein (772 amino acids)
additional information
-
recombinant expression of antisence Twm1 construct in Dictyostelium discoideum AX2 cells leading to mitochondrial dysfunction and reduced mtDNA copy number. Ethidium bromide exposure increases twm1 expression and results in mtDNA loss from which antisense transformants are less able to recover. Generation of a truncated Twm1 with 599 amino acids and 68 kDa, lacking the first 154 and last 19 amino acids of the full length protein (772 amino acids)
additional information
mtDNA helicase overexpression and knockdown, overexpression increases mtDNA copy number about 1.4fold while knockdown by RNA interference results in about 5fold decrease in mtDNA. Catalytic mutants analogous to A318 and D424 in the Walker A and B motifs in the helicase domain of T7 gp4, respectively, generate a dominant-negative, lethal phenotype resulting from a dramatic mtDNA depletion of 14-20fold. Mitochondrial transcript levels are reduced as a consequence of mtDNA depletion, but only after a 2fold decrease in mtDNA copy number is incurred. Overexpression of variants carrying analogous human-disease alleles in either the linker or C-terminal domain show differential effects. All are able to form hexamers in vivo, the I334P and A442P mutants (I367T and A475P in humans) show the lethal phenotype and mtDNA depletion found for the catalytic mutants, while A326T, R341Q, and W441C (A359T, R734Q, and W474C in humans) do not. Construction and evaluation of N-terminal domain-only variants of the Drosophila melanogaster homologue of human mtDNA helicase, the full-length NTD and its truncation variants in recombinant form are ssDNA-binding monomers
additional information
overexpression of the enzyme in Schneider S2 cells, elevated levels of mtDNA helicase alleviate pausing of the replication fork and increase the abundance of replication intermediates. The substantial increase in the signal of RIs in the absence of mtDNA copy number changes suggests that overexpression of mtDNA helicase promotes increased initiation without complete replication of mtDNA molecules. Circular molecules bear deletions in mtDNA from helicase overexpressing cells, elevated levels of mtDNA helicase promote rearrangement of the A+T region, mechanism, overview
additional information
-
overexpression of the enzyme in Schneider S2 cells, elevated levels of mtDNA helicase alleviate pausing of the replication fork and increase the abundance of replication intermediates. The substantial increase in the signal of RIs in the absence of mtDNA copy number changes suggests that overexpression of mtDNA helicase promotes increased initiation without complete replication of mtDNA molecules. Circular molecules bear deletions in mtDNA from helicase overexpressing cells, elevated levels of mtDNA helicase promote rearrangement of the A+T region, mechanism, overview
additional information
-
site-directed mutagenesis of the four conserved cysteines of the Fe-S cluster in the Rad3 (XPD) helicase from Ferroplasma acidarmanus (FacXPD) revealed that the integrity of the domain is required for the proper folding and structural stability of the auxiliary domain and is important for coupling ATP hydrolysis to unidirectional translocation of helicase
additional information
Fromanvirus D29
construction of a thioredoxin-tagged truncated version of WCGp80 protein, thio-DELTAN(1-189)WCGp80, in which the N-terminal sequences are removed, the mutant is fully capable of supporting helicase activity, although its ATP-dependence properties are altered, the substrate saturation curve for ATP in case of the mutant derivative is hyperbolic
additional information
-
His-tagged HDHB fragments incubated with glutathione beads bind to GST-RPA70N. HDHB residues 394-958 and 459-811 bind specifically to GST-RPA70N beads, demonstrating a specific interaction between HDHB 459-811 and RPA70N
additional information
enzyme inhibition by siRNA
additional information
-
enzyme inhibition by siRNA
additional information
ATP-dependent DNA unwinding increases about 50% with the overexpression of full-length enzyme from Twinkle gene in HEK-293 cells. The C-terminal region of human mtDNA helicase that is removed in T66 (66 kDa variant) represents an extension relative to the T7 gp4 polypeptide, and the further N-terminal deletion in T57 (57 kDA variant) at position K144 is consistent with the removal of the N-terminal zinc-binding domain (ZBD) in T7 gp4. An NTD only construct (DELTA372-684) shows no ATPase activity
additional information
-
ATP-dependent DNA unwinding increases about 50% with the overexpression of full-length enzyme from Twinkle gene in HEK-293 cells. The C-terminal region of human mtDNA helicase that is removed in T66 (66 kDa variant) represents an extension relative to the T7 gp4 polypeptide, and the further N-terminal deletion in T57 (57 kDA variant) at position K144 is consistent with the removal of the N-terminal zinc-binding domain (ZBD) in T7 gp4. An NTD only construct (DELTA372-684) shows no ATPase activity
additional information
depletion of the human DNA helicase B (HDHB) by shRNA silencing in U2-O2 cells, and microinjection of purified recombinant HDHB protein with a nonfunctional Walker B motif into cells in early G1/S. HDHB depletion prevents DNA synthesis, and the recombinant inactive mutant inhibits the G1/S transition. Thermolabile onset of S phase in mouse cells recombinantly expressing mutant HDHB and ability of injected Walker B mutant HDHB protein to block G1/S progression in human cells. Phenotypes, overview
additional information
-
depletion of the human DNA helicase B (HDHB) by shRNA silencing in U2-O2 cells, and microinjection of purified recombinant HDHB protein with a nonfunctional Walker B motif into cells in early G1/S. HDHB depletion prevents DNA synthesis, and the recombinant inactive mutant inhibits the G1/S transition. Thermolabile onset of S phase in mouse cells recombinantly expressing mutant HDHB and ability of injected Walker B mutant HDHB protein to block G1/S progression in human cells. Phenotypes, overview
additional information
generation of a TWINKLE mutant lacking the first 42 amino acids
additional information
-
generation of a TWINKLE mutant lacking the first 42 amino acids
additional information
generation of truncated enzyme forms, e.g. mutant DELTA277-286
additional information
in various human cellular systems, DDX11 downregulation by small interfering RNAs (siRNAs) causes a profound delay in mitotic progression leading to chromosome segregation anomalies and sister chromatid cohesion defects
additional information
-
in various human cellular systems, DDX11 downregulation by small interfering RNAs (siRNAs) causes a profound delay in mitotic progression leading to chromosome segregation anomalies and sister chromatid cohesion defects
additional information
-
construction of an intein-deleted form of DnaB
additional information
generation of a sen1DELTAN mutant strain and complemetation of the mutant with expression of the full-length wild-type SEN1 gene. The mutation in SEN1 affects the protein interactions and induce non-sexual flocculation in haploid mutant cells, flocculation phenotype, overview
additional information
-
generation of a sen1DELTAN mutant strain and complemetation of the mutant with expression of the full-length wild-type SEN1 gene. The mutation in SEN1 affects the protein interactions and induce non-sexual flocculation in haploid mutant cells, flocculation phenotype, overview
additional information
-
mutations of the Fe-S domain, including the conserved cysteines, abolishes SaXPD helicase activity and destabilizes tertiary structure, attesting to the structural importance of the Fe-S domain
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