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Literature summary for 5.6.2.3 extracted from

  • Singh, V.; Azad, G.K.; Sariki, S.K.; Tomar, R.S.
    Flocculation in Saccharomyces cerevisiae is regulated by RNA/DNA helicase Sen1p (2015), FEBS Lett., 589, 3165-3174 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
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 Saccharomyces cerevisiae
K128E site-directed mutagenesis, the mutation affects protein interactions, the mutant shows the flocculation phenotype Saccharomyces cerevisiae
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 Saccharomyces cerevisiae
R302W site-directed mutagenesis, the mutation affects protein interactions, the mutant shows an unaltered phenotype compared to wild-type Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
Saccharomyces cerevisiae 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Saccharomyces cerevisiae
-
ADP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q00416
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the C-terminal domain (CTD) of SEN1 is Ser5-phosphorylated as a component of the NNS complex. Glc7p can dephosphorylate Sen1p in vitro, which might affect NNS complex functionality Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
Saccharomyces cerevisiae ADP + phosphate
-
?

Synonyms

Synonyms Comment Organism
RNA/DNA helicase
-
Saccharomyces cerevisiae
SEN1
-
Saccharomyces cerevisiae
Sen1p
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution Sen1p is a nuclear superfamily 1 RNA/DNA helicase Saccharomyces cerevisiae
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 Saccharomyces cerevisiae
metabolism cooperative role of Rnt1p, Rrp6p and the Nrd1-Nab3-Sen1 (NNS) complex in the repression of flocculation FLO genes Saccharomyces cerevisiae
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 Saccharomyces cerevisiae