YOL021C - 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=S000005381 YOL021C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005381 YOL021C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''DIS3 ''

@@ Line 8: / Line 8: @@
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''DIS3 ''
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''RRP44''
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases'''           ||''MTR17, RRP44''
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type'''           || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XV:285427..282422
+|nowrap| Chr XV:285426..282421
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005381

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOL021C:''' Exosome core complex catalytic subunit; possesses both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase R and to human DIS3<ref name='S000054682'>Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem 123(5):883-90 {{SGDpaper|S000054682}} PMID 9562621</ref><ref name='S000129101'>Schaeffer D, et al. (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16(1):56-62 {{SGDpaper|S000129101}} PMID 19060898</ref><ref name='S000120270'>Liu Q, et al. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37 {{SGDpaper|S000120270}} PMID 17174896</ref><ref name='S000120282'>Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 {{SGDpaper|S000120282}} PMID 17173052</ref><ref name='S000125981'>Lorentzen E, et al. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29(6):717-28 {{SGDpaper|S000125981}} PMID 18374646</ref><ref name='S000128588'>Lebreton A, et al. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456(7224):993-6 {{SGDpaper|S000128588}} PMID 19060886</ref><ref name='S000128894'>Schneider C, et al. (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 37(4):1127-40
+'''Description of YOL021C:''' Exosome core complex catalytic subunit; possesses both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase R and to human DIS3<ref name='S000120282'>Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 {{SGDpaper|S000120282}} PMID 17173052</ref><ref name='S000128588'>Lebreton A, et al. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456(7224):993-6 {{SGDpaper|S000128588}} PMID 19060886</ref><ref name='S000120270'>Liu Q, et al. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37 {{SGDpaper|S000120270}} PMID 17174896</ref><ref name='S000125981'>Lorentzen E, et al. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29(6):717-28 {{SGDpaper|S000125981}} PMID 18374646</ref><ref name='S000129101'>Schaeffer D, et al. (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16(1):56-62 {{SGDpaper|S000129101}} PMID 19060898</ref><ref name='S000128894'>Schneider C, et al. (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 37(4):1127-40 {{SGDpaper|S000128894}} PMID 19129231</ref><ref name='S000054682'>Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem 123(5):883-90
-  {{SGDpaper|S000128894}} PMID 19129231</ref>
+  {{SGDpaper|S000054682}} PMID 9562621</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOL021C:''' Exosome core complex catalytic subunit; possesses both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase R and to human DIS3<ref name='S000129101'>Schaeffer D, et al. (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16(1):56-62 {{SGDpaper|S000129101}} PMID 19060898</ref><ref name='S000128894'>Schneider C, et al. (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 37(4):1127-40 {{SGDpaper|S000128894}} PMID 19129231</ref><ref name='S000128588'>Lebreton A, et al. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456(7224):993-6 {{SGDpaper|S000128588}} PMID 19060886</ref><ref name='S000125981'>Lorentzen E, et al. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29(6):717-28 {{SGDpaper|S000125981}} PMID 18374646</ref><ref name='S000120282'>Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 {{SGDpaper|S000120282}} PMID 17173052</ref><ref name='S000120270'>Liu Q, et al. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37 {{SGDpaper|S000120270}} PMID 17174896</ref><ref name='S000054682'>Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem 123(5):883-90
+'''Description of YOL021C:''' Exosome core complex catalytic subunit; possesses both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase R and to human DIS3<ref name='S000054682'>Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem 123(5):883-90 {{SGDpaper|S000054682}} PMID 9562621</ref><ref name='S000129101'>Schaeffer D, et al. (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16(1):56-62 {{SGDpaper|S000129101}} PMID 19060898</ref><ref name='S000120270'>Liu Q, et al. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37 {{SGDpaper|S000120270}} PMID 17174896</ref><ref name='S000120282'>Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 {{SGDpaper|S000120282}} PMID 17173052</ref><ref name='S000125981'>Lorentzen E, et al. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29(6):717-28 {{SGDpaper|S000125981}} PMID 18374646</ref><ref name='S000128588'>Lebreton A, et al. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456(7224):993-6 {{SGDpaper|S000128588}} PMID 19060886</ref><ref name='S000128894'>Schneider C, et al. (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 37(4):1127-40
-  {{SGDpaper|S000054682}} PMID 9562621</ref>
+  {{SGDpaper|S000128894}} PMID 19129231</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOL021C:''' Catalytic component of the exosome, involved in RNA processing and degradation; binds Gsp1p/Ran and enhances the GEF activity of Srm1p; implicated in mitotic control; homologous to the E. coli RNase R of the RNase II family<ref name='S000120282'>Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 {{SGDpaper|S000120282}} PMID 17173052</ref><ref name='S000060797'>Suzuki N, et al. (2001) The Saccharomyces cerevisiae small GTPase, Gsp1p/Ran, is involved in 3' processing of 7S-to-5.8S rRNA and in degradation of the excised 5'-A0 fragment of 35S pre-rRNA, both of which are carried out by the exosome. Genetics 158(2):613-25 {{SGDpaper|S000060797}} PMID 11404326</ref><ref name='S000059242'>Chekanova JA, et al. (2000) Poly(A) tail-dependent exonuclease AtRrp41p from Arabidopsis thaliana rescues 5.8 S rRNA processing and mRNA decay defects of the yeast ski6 mutant and is found in an exosome-sized complex in plant and yeast cells. J Biol Chem 275(42):33158-66 {{SGDpaper|S000059242}} PMID 10930416</ref><ref name='S000054682'>Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem (Tokyo) 123(5):883-90 {{SGDpaper|S000054682}} PMID 9562621</ref><ref name='S000049705'>Mitchell P, et al. (1997) The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'--&gt;5' exoribonucleases. Cell 91(4):457-66 {{SGDpaper|S000049705}} PMID 9390555</ref><ref name='S000043753'>Noguchi E, et al. (1996) Dis3, implicated in mitotic control, binds directly to Ran and enhances the GEF activity of RCC1. EMBO J 15(20):5595-605
+'''Description of YOL021C:''' Exosome core complex catalytic subunit; possesses both endonuclease and 3'-5' exonuclease activity; involved in 3'-5' RNA processing and degradation in both the nucleus and the cytoplasm; has similarity to E. coli RNase R and to human DIS3<ref name='S000129101'>Schaeffer D, et al. (2009) The exosome contains domains with specific endoribonuclease, exoribonuclease and cytoplasmic mRNA decay activities. Nat Struct Mol Biol 16(1):56-62 {{SGDpaper|S000129101}} PMID 19060898</ref><ref name='S000128894'>Schneider C, et al. (2009) The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res {{SGDpaper|S000128894}} PMID 19129231</ref><ref name='S000128588'>Lebreton A, et al. (2008) Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 456(7224):993-6 {{SGDpaper|S000128588}} PMID 19060886</ref><ref name='S000125981'>Lorentzen E, et al. (2008) Structure of the active subunit of the yeast exosome core, Rrp44: diverse modes of substrate recruitment in the RNase II nuclease family. Mol Cell 29(6):717-28 {{SGDpaper|S000125981}} PMID 18374646</ref><ref name='S000120282'>Dziembowski A, et al. (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22 {{SGDpaper|S000120282}} PMID 17173052</ref><ref name='S000120270'>Liu Q, et al. (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37 {{SGDpaper|S000120270}} PMID 17174896</ref><ref name='S000054682'>Shiomi T, et al. (1998) Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. J Biochem 123(5):883-90
-  {{SGDpaper|S000043753}} PMID 8896453</ref>
+  {{SGDpaper|S000054682}} PMID 9562621</ref>
 <br>
 <br>

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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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