YOR123C - Revision history

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{{PageTop}}
{|{{Prettytable}} align = 'right' width = '200px'
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YOR123C YOR123C]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''LEO1 ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Aliases''' ||'' ''
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Feature type''' || ORF, Verified[[Category:ORF]][[Category:ORF, Verified]]
|-
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
|nowrap| Chr XV:554571..553177
|-
|colspan = '3'|{{Don'tEditThisBox}}
|}
 
'''Description of {{PAGENAME}}:''' Component of the Paf1 complex, which associates with RNA polymerase II and is involved in histone methylation<ref name='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42 {{SGDpaper|S000074318}} PMID 12876294</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80
{{SGDpaper|S000069696}} PMID 11884586</ref>
 
 
 
 

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==Community Commentary==
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==References==

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@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOR123C:''' Component of the Paf1 complex, which associates with RNA polymerase II and is involved in histone methylation; plays a role in regulating Ty1 transposition<ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80 {{SGDpaper|S000069696}} PMID 11884586</ref><ref name='S000125260'>Nyswaner KM, et al. (2008) Chromatin-associated genes protect the yeast genome from ty1 insertional mutagenesis. Genetics 178(1):197-214 {{SGDpaper|S000125260}} PMID 18202368</ref><ref name='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42
+'''Description of YOR123C:''' Component of the Paf1 complex; which associates with RNA polymerase II and is involved in histone methylation; plays a role in regulating Ty1 transposition; involved in transcription elongation as demonstrated by the G-less-based run-on (GLRO) assay<ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80 {{SGDpaper|S000069696}} PMID 11884586</ref><ref name='S000125260'>Nyswaner KM, et al. (2008) Chromatin-associated genes protect the yeast genome from ty1 insertional mutagenesis. Genetics 178(1):197-214 {{SGDpaper|S000125260}} PMID 18202368</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='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42
   {{SGDpaper|S000074318}} PMID 12876294</ref>
 <br>

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XV:554571..553177
+|nowrap| Chr XV:554570..553176
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000005649

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOR123C:''' Component of the Paf1 complex, which associates with RNA polymerase II and is involved in histone methylation; plays a role in regulating Ty1 transposition<ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80 {{SGDpaper|S000069696}} PMID 11884586</ref><ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42 {{SGDpaper|S000074318}} PMID 12876294</ref><ref name='S000125260'>Nyswaner KM, et al. (2008) Chromatin-associated genes protect the yeast genome from ty1 insertional mutagenesis. Genetics 178(1):197-214
+'''Description of YOR123C:''' Component of the Paf1 complex, which associates with RNA polymerase II and is involved in histone methylation; plays a role in regulating Ty1 transposition<ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80 {{SGDpaper|S000069696}} PMID 11884586</ref><ref name='S000125260'>Nyswaner KM, et al. (2008) Chromatin-associated genes protect the yeast genome from ty1 insertional mutagenesis. Genetics 178(1):197-214 {{SGDpaper|S000125260}} PMID 18202368</ref><ref name='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42
-  {{SGDpaper|S000125260}} PMID 18202368</ref>
+  {{SGDpaper|S000074318}} PMID 12876294</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOR123C:''' Component of the Paf1 complex, which associates with RNA polymerase II and is involved in histone methylation; plays a role in regulating Ty1 transposition<ref name='S000125260'>Nyswaner KM, et al. (2008) Chromatin-associated genes protect the yeast genome from ty1 insertional mutagenesis. Genetics 178(1):197-214 {{SGDpaper|S000125260}} PMID 18202368</ref><ref name='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42 {{SGDpaper|S000074318}} PMID 12876294</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80
+'''Description of YOR123C:''' Component of the Paf1 complex, which associates with RNA polymerase II and is involved in histone methylation; plays a role in regulating Ty1 transposition<ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80 {{SGDpaper|S000069696}} PMID 11884586</ref><ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42 {{SGDpaper|S000074318}} PMID 12876294</ref><ref name='S000125260'>Nyswaner KM, et al. (2008) Chromatin-associated genes protect the yeast genome from ty1 insertional mutagenesis. Genetics 178(1):197-214
-  {{SGDpaper|S000069696}} PMID 11884586</ref>
+  {{SGDpaper|S000125260}} PMID 18202368</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YOR123C:''' Component of the Paf1 complex, which associates with RNA polymerase II and is involved in histone methylation<ref name='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42 {{SGDpaper|S000074318}} PMID 12876294</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80
+'''Description of YOR123C:''' Component of the Paf1 complex, which associates with RNA polymerase II and is involved in histone methylation; plays a role in regulating Ty1 transposition<ref name='S000125260'>Nyswaner KM, et al. (2008) Chromatin-associated genes protect the yeast genome from ty1 insertional mutagenesis. Genetics 178(1):197-214 {{SGDpaper|S000125260}} PMID 18202368</ref><ref name='S000074318'>Wood A, et al. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J Biol Chem 278(37):34739-42 {{SGDpaper|S000074318}} PMID 12876294</ref><ref name='S000073147'>Krogan NJ, et al. (2003) The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation. Mol Cell 11(3):721-9 {{SGDpaper|S000073147}} PMID 12667454</ref><ref name='S000071874'>Betz JL, et al. (2002) Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism. Mol Genet Genomics 268(2):272-85 {{SGDpaper|S000071874}} PMID 12395202</ref><ref name='S000069696'>Mueller CL and Jaehning JA (2002) Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol Cell Biol 22(7):1971-80
   {{SGDpaper|S000069696}} PMID 11884586</ref>
 <br>

@@ 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=S000005649 YOR123C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000005649 YOR123C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''LEO1 ''

← 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 -->
		+	<!--
		+	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>
		+	-->

	<protect>		<protect>

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 {|{{Prettytable}} align = 'right' width = '200px'
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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XV:554571..553177
 |}
 <br>
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+<br>
 __TOC__
 ==Community Commentary==
 {{CommentaryHelp}}
 ==References==
 <!-- REFERENCES ARE AUTOMATICALLY GENERATED.  PLEASE DON'T EDIT THIS SECTION-->
 {{RefHelp}}