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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
nucleus | - |
Saccharomyces cerevisiae | 5634 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | Saccharomyces cerevisiae | - |
ADP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q00416 | - |
- |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RNA/DNA helicase | - |
Saccharomyces cerevisiae |
SEN1 | - |
Saccharomyces cerevisiae |
Sen1p | - |
Saccharomyces cerevisiae |
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 |