Difference between revisions of "YOR001W"
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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=S000005527 YOR001W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RRP6 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''RRP6 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr XV: | + | |nowrap| Chr XV:326832..329033 |
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| − | | | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000005527 |
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| − | '''Description of | + | '''Description of YOR001W:''' Nuclear exosome exonuclease component; has 3'-5' exonuclease activity; involved in RNA processing, maturation, surveillance, degradation, tethering, and export; has similarity to E. coli RNase D and to human PM-Sc1 100 (EXOSC10); mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay<ref name='S000074753'>Bousquet-Antonelli C, et al. (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102(6):765-75 {{SGDpaper|S000074753}} PMID 11030620</ref><ref name='S000042261'>Briggs MW, et al. (1998) Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3' end formation. J Biol Chem 273(21):13255-63 {{SGDpaper|S000042261}} PMID 9582370</ref><ref name='S000043381'>Burkard KT and Butler JS (2000) A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p. Mol Cell Biol 20(2):604-16 {{SGDpaper|S000043381}} PMID 10611239</ref><ref name='S000077467'>Hieronymus H, et al. (2004) Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18(21):2652-62 {{SGDpaper|S000077467}} PMID 15489286</ref><ref name='S000065959'>Hilleren P, et al. (2001) Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 413(6855):538-42 {{SGDpaper|S000065959}} PMID 11586364</ref><ref name='S000146226'>Tous C, et al. (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64 {{SGDpaper|S000146226}} PMID 21478823</ref><ref name='S000126973'>Vodala S, et al. (2008) The nuclear exosome and adenylation regulate posttranscriptional tethering of yeast GAL genes to the nuclear periphery. Mol Cell 31(1):104-13 |
| − | {{SGDpaper| | + | {{SGDpaper|S000126973}} PMID 18614049</ref> |
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==Community Commentary== | ==Community Commentary== | ||
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| + | === Protein Details === | ||
| + | [[Category:Topic:Protein Details]] | ||
| + | ==== Protein Modification ==== | ||
| + | [[Category:Topic:Protein Details:Protein Modification]] | ||
| + | '''Modification(s)''': Phosphorylation [[Category:Modification:Phosphorylation]] | ||
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| + | Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. <ref name='S000074306'>Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 {{SGDpaper|S000074306}} PMID 14574415</ref> <ref name = 'CAset7903-2004-01-29'>submitted by [http://db.yeastgenome.org/cgi-bin/colleague/colleagueSearch?id=7903 Jeff Ubersax] on 2004-01-29</ref> | ||
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| + | Specifically higher expression in carbon limited chemostat cultures versus carbon excess. | ||
| + | <ref>Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. | ||
| + | J Biol Chem 278(5):3265-74</ref> | ||
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==References== | ==References== | ||
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Latest revision as of 06:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YOR001W |
| Gene name | RRP6 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XV:326832..329033 |
| Primary SGDID | S000005527 |
Description of YOR001W: Nuclear exosome exonuclease component; has 3'-5' exonuclease activity; involved in RNA processing, maturation, surveillance, degradation, tethering, and export; has similarity to E. coli RNase D and to human PM-Sc1 100 (EXOSC10); mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay[1][2][3][4][5][6][7]
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Community Commentary
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Protein Details
Protein Modification
Modification(s): Phosphorylation
Identified as an efficient substrate of Clb2-Cdk1-as1 in a screen of a proteomic GST-fusion library. [8] [9]
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References
See Help:References on how to add references
- ↑ Bousquet-Antonelli C, et al. (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102(6):765-75 SGD PMID 11030620
- ↑ Briggs MW, et al. (1998) Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3' end formation. J Biol Chem 273(21):13255-63 SGD PMID 9582370
- ↑ Burkard KT and Butler JS (2000) A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p. Mol Cell Biol 20(2):604-16 SGD PMID 10611239
- ↑ Hieronymus H, et al. (2004) Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18(21):2652-62 SGD PMID 15489286
- ↑ Hilleren P, et al. (2001) Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 413(6855):538-42 SGD PMID 11586364
- ↑ Tous C, et al. (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64 SGD PMID 21478823
- ↑ Vodala S, et al. (2008) The nuclear exosome and adenylation regulate posttranscriptional tethering of yeast GAL genes to the nuclear periphery. Mol Cell 31(1):104-13 SGD PMID 18614049
- ↑ Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 SGD PMID 14574415
- ↑ submitted by Jeff Ubersax on 2004-01-29
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