Difference between revisions of "YOR001W"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YOR001W YOR001W]  
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|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'''
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|nowrap| Chr XV:326833..329034
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|nowrap| Chr XV:326832..329033
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''          || S000005527
 
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'''Description of {{PAGENAME}}:''' Exonuclease component of the nuclear exosome; contributes to the quality-control system that retains and degrades aberrant mRNAs in the nucleus<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='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='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='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
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'''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
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  {{SGDpaper|S000126973}} PMID 18614049</ref>
 
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=== Protein Details ===
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==== Protein Modification ====
 
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'''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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==Community Commentary==
 
==Community Commentary==
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Specifically higher expression in carbon limited chemostat cultures versus carbon excess.
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<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.
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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

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  1. ↑ Bousquet-Antonelli C, et al. (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102(6):765-75 SGD PMID 11030620
  2. ↑ 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
  3. ↑ 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
  4. ↑ Hieronymus H, et al. (2004) Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18(21):2652-62 SGD PMID 15489286
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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
  8. ↑ Ubersax JA, et al. (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64 SGD PMID 14574415
  9. ↑ submitted by Jeff Ubersax on 2004-01-29

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