YDR258C - 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=S000002666 YDR258C]
+|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002666 YDR258C]
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''         ||''HSP78 ''

@@ Line 13: / Line 13: @@
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates'''
-|nowrap| Chr IV:974240..971805
+|nowrap| Chr IV:974243..971808
 |-
 |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID'''           || S000002666

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR258C:''' Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates<ref name='S000039663'>Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44 {{SGDpaper|S000039663}} PMID 7628444</ref><ref name='S000040952'>Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 {{SGDpaper|S000040952}} PMID 8413229</ref><ref name='S000047871'>Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 {{SGDpaper|S000047871}} PMID 7500331</ref><ref name='S000050221'>Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 {{SGDpaper|S000050221}} PMID 8830768</ref><ref name='S000114353'>von Janowsky B, et al. (2006) The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J Mol Biol 357(3):793-807 {{SGDpaper|S000114353}} PMID 16460754</ref><ref name='S000070276'>Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 {{SGDpaper|S000070276}} PMID 12023279</ref><ref name='S000072044'>Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37
+'''Description of YDR258C:''' Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates<ref name='S000070276'>Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 {{SGDpaper|S000070276}} PMID 12023279</ref><ref name='S000040952'>Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 {{SGDpaper|S000040952}} PMID 8413229</ref><ref name='S000047871'>Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 {{SGDpaper|S000047871}} PMID 7500331</ref><ref name='S000072044'>Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37 {{SGDpaper|S000072044}} PMID 12237310</ref><ref name='S000039663'>Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44 {{SGDpaper|S000039663}} PMID 7628444</ref><ref name='S000050221'>Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 {{SGDpaper|S000050221}} PMID 8830768</ref><ref name='S000114353'>von Janowsky B, et al. (2006) The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J Mol Biol 357(3):793-807
-  {{SGDpaper|S000072044}} PMID 12237310</ref>
+  {{SGDpaper|S000114353}} PMID 16460754</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR258C:''' Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates<ref name='S000114353'>von Janowsky B, et al. (2006) The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J Mol Biol 357(3):793-807 {{SGDpaper|S000114353}} PMID 16460754</ref><ref name='S000072044'>Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37 {{SGDpaper|S000072044}} PMID 12237310</ref><ref name='S000070276'>Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 {{SGDpaper|S000070276}} PMID 12023279</ref><ref name='S000050221'>Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 {{SGDpaper|S000050221}} PMID 8830768</ref><ref name='S000047871'>Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 {{SGDpaper|S000047871}} PMID 7500331</ref><ref name='S000040952'>Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 {{SGDpaper|S000040952}} PMID 8413229</ref><ref name='S000039663'>Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44
+'''Description of YDR258C:''' Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates<ref name='S000039663'>Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44 {{SGDpaper|S000039663}} PMID 7628444</ref><ref name='S000040952'>Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 {{SGDpaper|S000040952}} PMID 8413229</ref><ref name='S000047871'>Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 {{SGDpaper|S000047871}} PMID 7500331</ref><ref name='S000050221'>Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 {{SGDpaper|S000050221}} PMID 8830768</ref><ref name='S000114353'>von Janowsky B, et al. (2006) The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J Mol Biol 357(3):793-807 {{SGDpaper|S000114353}} PMID 16460754</ref><ref name='S000070276'>Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 {{SGDpaper|S000070276}} PMID 12023279</ref><ref name='S000072044'>Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37
-  {{SGDpaper|S000039663}} PMID 7628444</ref>
+  {{SGDpaper|S000072044}} PMID 12237310</ref>
 <br>
 <br>

@@ Line 18: / Line 18: @@
 |}
 <br>
-'''Description of YDR258C:''' Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; prevents the aggregation of misfolded matrix proteins; component of the mitochondrial proteolysis system<ref name='S000072044'>Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37 {{SGDpaper|S000072044}} PMID 12237310</ref><ref name='S000070276'>Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 {{SGDpaper|S000070276}} PMID 12023279</ref><ref name='S000050221'>Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 {{SGDpaper|S000050221}} PMID 8830768</ref><ref name='S000047871'>Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 {{SGDpaper|S000047871}} PMID 7500331</ref><ref name='S000040952'>Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 {{SGDpaper|S000040952}} PMID 8413229</ref><ref name='S000039663'>Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44
+'''Description of YDR258C:''' Oligomeric mitochondrial matrix chaperone that cooperates with Ssc1p in mitochondrial thermotolerance after heat shock; able to prevent the aggregation of misfolded proteins as well as resolubilize protein aggregates<ref name='S000114353'>von Janowsky B, et al. (2006) The disaggregation activity of the mitochondrial ClpB homolog Hsp78 maintains Hsp70 function during heat stress. J Mol Biol 357(3):793-807 {{SGDpaper|S000114353}} PMID 16460754</ref><ref name='S000072044'>Rottgers K, et al. (2002) The ClpB homolog Hsp78 is required for the efficient degradation of proteins in the mitochondrial matrix. J Biol Chem 277(48):45829-37 {{SGDpaper|S000072044}} PMID 12237310</ref><ref name='S000070276'>Germaniuk A, et al. (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8 {{SGDpaper|S000070276}} PMID 12023279</ref><ref name='S000050221'>Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 {{SGDpaper|S000050221}} PMID 8830768</ref><ref name='S000047871'>Moczko M, et al. (1995) The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function. J Mol Biol 254(4):538-43 {{SGDpaper|S000047871}} PMID 7500331</ref><ref name='S000040952'>Leonhardt SA, et al. (1993) HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13(10):6304-13 {{SGDpaper|S000040952}} PMID 8413229</ref><ref name='S000039663'>Schmitt M, et al. (1995) Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14(14):3434-44
   {{SGDpaper|S000039663}} PMID 7628444</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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