YOR001W - Revision history

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@@ Line 4: / Line 4: @@
 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005527 YOR001W]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005527 YOR001W]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''RRP6 ''

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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)<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='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
+'''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|S000126973}} PMID 18614049</ref>
 <br>

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 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XV:326833..329034
+|nowrap| Chr XV:326832..329033
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005527

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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)<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='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='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
+'''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)<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='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|S000126973}} PMID 18614049</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''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)<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|S000126973}} PMID 18614049</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='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
+'''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)<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='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='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|S000042261}} PMID 9582370</ref>
+  {{SGDpaper|S000126973}} PMID 18614049</ref>
 <br>
 <br>

← Older revision		Revision as of 20:02, 21 February 2007
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		+	<!-- PLEASE ADD Community Commentary ABOVE THIS MESSAGE. See below for an example of community annotation -->
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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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 {|{{Prettytable}} align = 'right' width = '200px'
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XV:326833..329034
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 ==Community Commentary==
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