YMR145C - Revision history

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 {|{{Prettytable}} align = 'right' width = '200px'
 |-
-|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004753 YMR145C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000004753 YMR145C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''NDE1 ''

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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr XIII:556474..554792
+|nowrap| Chr XIII:556475..554793
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000004753

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR145C:''' Mitochondrial external NADH dehydrogenase, a type II NAD(P)H:quinone oxidoreductase that catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p provide cytosolic NADH to the mitochondrial respiratory chain<ref name='S000039774'>Overkamp KM, et al. (2000) In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J Bacteriol 182(10):2823-30 {{SGDpaper|S000039774}} PMID 10781551</ref><ref name='S000040550'>Luttik MA, et al. (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273(38):24529-34 {{SGDpaper|S000040550}} PMID 9733747</ref><ref name='S000042730'>Small WC and McAlister-Henn L (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 180(16):4051-5 {{SGDpaper|S000042730}} PMID 9696750</ref><ref name='S000079980'>Melo AM, et al. (2004) New insights into type II NAD(P)H:quinone oxidoreductases. Microbiol Mol Biol Rev 68(4):603-16 {{SGDpaper|S000079980}} PMID 15590775</ref><ref name='S000070271'>Pahlman IL, et al. (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5
+'''Description of YMR145C:''' Mitochondrial external NADH dehydrogenase, a type II NAD(P)H:quinone oxidoreductase that catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p provide cytosolic NADH to the mitochondrial respiratory chain<ref name='S000040550'>Luttik MA, et al. (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273(38):24529-34 {{SGDpaper|S000040550}} PMID 9733747</ref><ref name='S000079980'>Melo AM, et al. (2004) New insights into type II NAD(P)H:quinone oxidoreductases. Microbiol Mol Biol Rev 68(4):603-16 {{SGDpaper|S000079980}} PMID 15590775</ref><ref name='S000039774'>Overkamp KM, et al. (2000) In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J Bacteriol 182(10):2823-30 {{SGDpaper|S000039774}} PMID 10781551</ref><ref name='S000070271'>Pahlman IL, et al. (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5 {{SGDpaper|S000070271}} PMID 12032156</ref><ref name='S000042730'>Small WC and McAlister-Henn L (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 180(16):4051-5
-  {{SGDpaper|S000070271}} PMID 12032156</ref>
+  {{SGDpaper|S000042730}} PMID 9696750</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR145C:''' Mitochondrial external NADH dehydrogenase, a type II NAD(P)H:quinone oxidoreductase that catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p provide cytosolic NADH to the mitochondrial respiratory chain<ref name='S000079980'>Melo AM, et al. (2004) New insights into type II NAD(P)H:quinone oxidoreductases. Microbiol Mol Biol Rev 68(4):603-16 {{SGDpaper|S000079980}} PMID 15590775</ref><ref name='S000070271'>Pahlman IL, et al. (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5 {{SGDpaper|S000070271}} PMID 12032156</ref><ref name='S000042730'>Small WC and McAlister-Henn L (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 180(16):4051-5 {{SGDpaper|S000042730}} PMID 9696750</ref><ref name='S000040550'>Luttik MA, et al. (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273(38):24529-34 {{SGDpaper|S000040550}} PMID 9733747</ref><ref name='S000039774'>Overkamp KM, et al. (2000) In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J Bacteriol 182(10):2823-30
+'''Description of YMR145C:''' Mitochondrial external NADH dehydrogenase, a type II NAD(P)H:quinone oxidoreductase that catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p provide cytosolic NADH to the mitochondrial respiratory chain<ref name='S000039774'>Overkamp KM, et al. (2000) In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J Bacteriol 182(10):2823-30 {{SGDpaper|S000039774}} PMID 10781551</ref><ref name='S000040550'>Luttik MA, et al. (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273(38):24529-34 {{SGDpaper|S000040550}} PMID 9733747</ref><ref name='S000042730'>Small WC and McAlister-Henn L (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 180(16):4051-5 {{SGDpaper|S000042730}} PMID 9696750</ref><ref name='S000079980'>Melo AM, et al. (2004) New insights into type II NAD(P)H:quinone oxidoreductases. Microbiol Mol Biol Rev 68(4):603-16 {{SGDpaper|S000079980}} PMID 15590775</ref><ref name='S000070271'>Pahlman IL, et al. (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5
-  {{SGDpaper|S000039774}} PMID 10781551</ref>
+  {{SGDpaper|S000070271}} PMID 12032156</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YMR145C:''' Mitochondrial external NADH dehydrogenase, catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p are involved in providing the cytosolic NADH to the mitochondrial respiratory chain<ref name='S000070271'>Pahlman IL, et al. (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5 {{SGDpaper|S000070271}} PMID 12032156</ref><ref name='S000042730'>Small WC and McAlister-Henn L (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 180(16):4051-5 {{SGDpaper|S000042730}} PMID 9696750</ref><ref name='S000040550'>Luttik MA, et al. (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273(38):24529-34 {{SGDpaper|S000040550}} PMID 9733747</ref><ref name='S000039774'>Overkamp KM, et al. (2000) In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J Bacteriol 182(10):2823-30
+'''Description of YMR145C:''' Mitochondrial external NADH dehydrogenase, a type II NAD(P)H:quinone oxidoreductase that catalyzes the oxidation of cytosolic NADH; Nde1p and Nde2p provide cytosolic NADH to the mitochondrial respiratory chain<ref name='S000079980'>Melo AM, et al. (2004) New insights into type II NAD(P)H:quinone oxidoreductases. Microbiol Mol Biol Rev 68(4):603-16 {{SGDpaper|S000079980}} PMID 15590775</ref><ref name='S000070271'>Pahlman IL, et al. (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5 {{SGDpaper|S000070271}} PMID 12032156</ref><ref name='S000042730'>Small WC and McAlister-Henn L (1998) Identification of a cytosolically directed NADH dehydrogenase in mitochondria of Saccharomyces cerevisiae. J Bacteriol 180(16):4051-5 {{SGDpaper|S000042730}} PMID 9696750</ref><ref name='S000040550'>Luttik MA, et al. (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273(38):24529-34 {{SGDpaper|S000040550}} PMID 9733747</ref><ref name='S000039774'>Overkamp KM, et al. (2000) In vivo analysis of the mechanisms for oxidation of cytosolic NADH by Saccharomyces cerevisiae mitochondria. J Bacteriol 182(10):2823-30
   {{SGDpaper|S000039774}} PMID 10781551</ref>
 <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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 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
 |nowrap| Chr XIII:556474..554792
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