YDR529C - 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=S000002937 YDR529C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002937 YDR529C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''QCR7 ''

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 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr IV:1496541..1496158
+|nowrap| Chr IV:1496548..1496165
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000002937

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR529C:''' Subunit 7 of the ubiquinol cytochrome-c reductase complex, which is a component of the mitochondrial inner membrane electron transport chain; oriented facing the mitochondrial matrix; N-terminus appears to play a role in complex assembly<ref name='S000056774'>Hemrika W and Berden JA (1990) Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. Eur J Biochem 192(3):761-5 {{SGDpaper|S000056774}} PMID 2170131</ref><ref name='S000057248'>De Haan M, et al. (1984) The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit. Eur J Biochem 138(1):169-77 {{SGDpaper|S000057248}} PMID 6319130</ref><ref name='S000066042'>Lee SY, et al. (2001) The N-terminus of the Qcr7 protein of the cytochrome bc(1) complex in S. cerevisiae may be involved in facilitating stability of the subcomplex with the Qcr8 protein and cytochrome b. Arch Biochem Biophys 393(2):215-21
+'''Description of YDR529C:''' Subunit 7 of the ubiquinol cytochrome-c reductase complex, which is a component of the mitochondrial inner membrane electron transport chain; oriented facing the mitochondrial matrix; N-terminus appears to play a role in complex assembly<ref name='S000057248'>De Haan M, et al. (1984) The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit. Eur J Biochem 138(1):169-77 {{SGDpaper|S000057248}} PMID 6319130</ref><ref name='S000056774'>Hemrika W and Berden JA (1990) Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. Eur J Biochem 192(3):761-5 {{SGDpaper|S000056774}} PMID 2170131</ref><ref name='S000066042'>Lee SY, et al. (2001) The N-terminus of the Qcr7 protein of the cytochrome bc(1) complex in S. cerevisiae may be involved in facilitating stability of the subcomplex with the Qcr8 protein and cytochrome b. Arch Biochem Biophys 393(2):215-21
   {{SGDpaper|S000066042}} PMID 11556808</ref>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR529C:''' Subunit 7 of the ubiquinol cytochrome-c reductase complex, which is a component of the mitochondrial inner membrane electron transport chain; oriented facing the mitochondrial matrix; N-terminus appears to play a role in complex assembly<ref name='S000066042'>Lee SY, et al. (2001) The N-terminus of the Qcr7 protein of the cytochrome bc(1) complex in S. cerevisiae may be involved in facilitating stability of the subcomplex with the Qcr8 protein and cytochrome b. Arch Biochem Biophys 393(2):215-21 {{SGDpaper|S000066042}} PMID 11556808</ref><ref name='S000057248'>De Haan M, et al. (1984) The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit. Eur J Biochem 138(1):169-77 {{SGDpaper|S000057248}} PMID 6319130</ref><ref name='S000056774'>Hemrika W and Berden JA (1990) Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. Eur J Biochem 192(3):761-5
+'''Description of YDR529C:''' Subunit 7 of the ubiquinol cytochrome-c reductase complex, which is a component of the mitochondrial inner membrane electron transport chain; oriented facing the mitochondrial matrix; N-terminus appears to play a role in complex assembly<ref name='S000056774'>Hemrika W and Berden JA (1990) Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. Eur J Biochem 192(3):761-5 {{SGDpaper|S000056774}} PMID 2170131</ref><ref name='S000057248'>De Haan M, et al. (1984) The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit. Eur J Biochem 138(1):169-77 {{SGDpaper|S000057248}} PMID 6319130</ref><ref name='S000066042'>Lee SY, et al. (2001) The N-terminus of the Qcr7 protein of the cytochrome bc(1) complex in S. cerevisiae may be involved in facilitating stability of the subcomplex with the Qcr8 protein and cytochrome b. Arch Biochem Biophys 393(2):215-21
-  {{SGDpaper|S000056774}} PMID 2170131</ref>
+  {{SGDpaper|S000066042}} PMID 11556808</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR529C:''' Subunit 7 of the ubiquinol cytochrome-c reductase complex, which is a component of the mitochondrial inner membrane electron transport chain; oriented facing the mitochondrial matrix; N-terminus appears to play a role in complex assembly<ref name='S000056774'>Hemrika W and Berden JA (1990) Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. Eur J Biochem 192(3):761-5 {{SGDpaper|S000056774}} PMID 2170131</ref><ref name='S000057248'>De Haan M, et al. (1984) The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit. Eur J Biochem 138(1):169-77 {{SGDpaper|S000057248}} PMID 6319130</ref><ref name='S000066042'>Lee SY, et al. (2001) The N-terminus of the Qcr7 protein of the cytochrome bc(1) complex in S. cerevisiae may be involved in facilitating stability of the subcomplex with the Qcr8 protein and cytochrome b. Arch Biochem Biophys 393(2):215-21
+'''Description of YDR529C:''' Subunit 7 of the ubiquinol cytochrome-c reductase complex, which is a component of the mitochondrial inner membrane electron transport chain; oriented facing the mitochondrial matrix; N-terminus appears to play a role in complex assembly<ref name='S000066042'>Lee SY, et al. (2001) The N-terminus of the Qcr7 protein of the cytochrome bc(1) complex in S. cerevisiae may be involved in facilitating stability of the subcomplex with the Qcr8 protein and cytochrome b. Arch Biochem Biophys 393(2):215-21 {{SGDpaper|S000066042}} PMID 11556808</ref><ref name='S000057248'>De Haan M, et al. (1984) The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit. Eur J Biochem 138(1):169-77 {{SGDpaper|S000057248}} PMID 6319130</ref><ref name='S000056774'>Hemrika W and Berden JA (1990) Membrane topography of the subunits of ubiquinol-cytochrome-c oxidoreductase of Saccharomyces cerevisiae. The 14-kDa and the 11-kDa subunits face opposite sides of the mitochondrial inner membrane. Eur J Biochem 192(3):761-5
-  {{SGDpaper|S000066042}} PMID 11556808</ref>
+  {{SGDpaper|S000056774}} PMID 2170131</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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	<protect>		<protect>

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr IV:1496540..1496157
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