Difference between revisions of "YNL251C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005195 YNL251C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''NRD1 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''NRD1 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XIV: | + | |nowrap| Chr XIV:174315..172588 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005195 | ||
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| − | '''Description of | + | '''Description of YNL251C:''' RNA-binding protein, subunit of Nrd1 complex (Nrd1p-Nab3p-Sen1p); complex interacts with the exosome to mediate 3′ end formation of some mRNAs, snRNAs, snoRNAs, and CUTs; interacts with the C-terminal domain of the RNA polymerase II large subunit (Rpo21p), preferentially at phosphorylated Ser5, to direct transcription termination of non-polyadenylated transcripts; H3K4 trimethylation of transcribed regions by Set1p enhances recruitment of Nrd1p to those sites<ref name='S000045868'>Conrad NK, et al. (2000) A yeast heterogeneous nuclear ribonucleoprotein complex associated with RNA polymerase II. Genetics 154(2):557-71 {{SGDpaper|S000045868}} PMID 10655211</ref><ref name='S000052606'>Steinmetz EJ and Brow DA (1998) Control of pre-mRNA accumulation by the essential yeast protein Nrd1 requires high-affinity transcript binding and a domain implicated in RNA polymerase II association. Proc Natl Acad Sci U S A 95(12):6699-704 {{SGDpaper|S000052606}} PMID 9618475</ref><ref name='S000071624'>Steinmetz EJ, et al. (2001) RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of RNA polymerase II transcripts. Nature 413(6853):327-31 {{SGDpaper|S000071624}} PMID 11565036</ref><ref name='S000145879'>Terzi N, et al. (2011) H3K4 trimethylation by Set1 promotes efficient termination by the Nrd1-Nab3-Sen1 pathway. Mol Cell Biol () {{SGDpaper|S000145879}} PMID 21709022</ref><ref name='S000127231'>Vasiljeva L, et al. (2008) The Nrd1-Nab3-Sen1 termination complex interacts with the Ser5-phosphorylated RNA polymerase II C-terminal domain. Nat Struct Mol Biol 15(8):795-804 |
| − | {{SGDpaper| | + | {{SGDpaper|S000127231}} PMID 18660819</ref> |
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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Latest revision as of 14:05, 11 October 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YNL251C |
| Gene name | NRD1 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XIV:174315..172588 |
| Primary SGDID | S000005195 |
Description of YNL251C: RNA-binding protein, subunit of Nrd1 complex (Nrd1p-Nab3p-Sen1p); complex interacts with the exosome to mediate 3′ end formation of some mRNAs, snRNAs, snoRNAs, and CUTs; interacts with the C-terminal domain of the RNA polymerase II large subunit (Rpo21p), preferentially at phosphorylated Ser5, to direct transcription termination of non-polyadenylated transcripts; H3K4 trimethylation of transcribed regions by Set1p enhances recruitment of Nrd1p to those sites[1][2][3][4][5]
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References
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- ↑ Conrad NK, et al. (2000) A yeast heterogeneous nuclear ribonucleoprotein complex associated with RNA polymerase II. Genetics 154(2):557-71 SGD PMID 10655211
- ↑ Steinmetz EJ and Brow DA (1998) Control of pre-mRNA accumulation by the essential yeast protein Nrd1 requires high-affinity transcript binding and a domain implicated in RNA polymerase II association. Proc Natl Acad Sci U S A 95(12):6699-704 SGD PMID 9618475
- ↑ Steinmetz EJ, et al. (2001) RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of RNA polymerase II transcripts. Nature 413(6853):327-31 SGD PMID 11565036
- ↑ Terzi N, et al. (2011) H3K4 trimethylation by Set1 promotes efficient termination by the Nrd1-Nab3-Sen1 pathway. Mol Cell Biol () SGD PMID 21709022
- ↑ Vasiljeva L, et al. (2008) The Nrd1-Nab3-Sen1 termination complex interacts with the Ser5-phosphorylated RNA polymerase II C-terminal domain. Nat Struct Mol Biol 15(8):795-804 SGD PMID 18660819
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