YFL016C - 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=S000001878 YFL016C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000001878 YFL016C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''MDJ1 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr VI:106230..104695
+|nowrap| Chr VI:106236..104701
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000001878

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YFL016C:''' Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones<ref name='S000044393'>Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71 {{SGDpaper|S000044393}} PMID 8943361</ref><ref name='S000044484'>Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 {{SGDpaper|S000044484}} PMID 7957078</ref><ref name='S000046349'>Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 {{SGDpaper|S000046349}} PMID 9973563</ref><ref name='S000048831'>Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59
+'''Description of YFL016C:''' Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones<ref name='S000046349'>Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 {{SGDpaper|S000046349}} PMID 9973563</ref><ref name='S000048831'>Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59 {{SGDpaper|S000048831}} PMID 8168133</ref><ref name='S000044484'>Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 {{SGDpaper|S000044484}} PMID 7957078</ref><ref name='S000044393'>Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71
-  {{SGDpaper|S000048831}} PMID 8168133</ref>
+  {{SGDpaper|S000044393}} PMID 8943361</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YFL016C:''' Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones<ref name='S000048831'>Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59 {{SGDpaper|S000048831}} PMID 8168133</ref><ref name='S000046349'>Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 {{SGDpaper|S000046349}} PMID 9973563</ref><ref name='S000044484'>Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 {{SGDpaper|S000044484}} PMID 7957078</ref><ref name='S000044393'>Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71
+'''Description of YFL016C:''' Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones<ref name='S000044393'>Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71 {{SGDpaper|S000044393}} PMID 8943361</ref><ref name='S000044484'>Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 {{SGDpaper|S000044484}} PMID 7957078</ref><ref name='S000046349'>Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 {{SGDpaper|S000046349}} PMID 9973563</ref><ref name='S000048831'>Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59
-  {{SGDpaper|S000044393}} PMID 8943361</ref>
+  {{SGDpaper|S000048831}} PMID 8168133</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YFL016C:''' Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones<ref name='S000044393'>Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71 {{SGDpaper|S000044393}} PMID 8943361</ref><ref name='S000044484'>Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 {{SGDpaper|S000044484}} PMID 7957078</ref><ref name='S000046349'>Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 {{SGDpaper|S000046349}} PMID 9973563</ref><ref name='S000048831'>Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59
+'''Description of YFL016C:''' Co-chaperone that stimulates the ATPase activity of the HSP70 protein Ssc1p; involved in protein folding/refolding in the mitochodrial matrix; required for proteolysis of misfolded proteins; member of the HSP40 (DnaJ) family of chaperones<ref name='S000048831'>Rowley N, et al. (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59 {{SGDpaper|S000048831}} PMID 8168133</ref><ref name='S000046349'>Kubo Y, et al. (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64 {{SGDpaper|S000046349}} PMID 9973563</ref><ref name='S000044484'>Wagner I, et al. (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45 {{SGDpaper|S000044484}} PMID 7957078</ref><ref name='S000044393'>Westermann B, et al. (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71
-  {{SGDpaper|S000048831}} PMID 8168133</ref>
+  {{SGDpaper|S000044393}} PMID 8943361</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 -->
		+	<!--
		+	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 VI:106230..104695
 |}
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 ==Community Commentary==
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