Difference between revisions of "YDR258C"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http:// | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002666 YDR258C] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP78 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''HSP78 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
| − | |nowrap| Chr IV: | + | |nowrap| Chr IV:974243..971808 |
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002666 | ||
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| − | '''Description of | + | '''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| | + | {{SGDpaper|S000114353}} PMID 16460754</ref> |
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==Community Commentary== | ==Community Commentary== | ||
{{CommentaryHelp}} | {{CommentaryHelp}} | ||
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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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Latest revision as of 07:45, 23 January 2012
Share your knowledge...Edit this entry! <protect>
| Systematic name | YDR258C |
| Gene name | HSP78 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:974243..971808 |
| Primary SGDID | S000002666 |
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[1][2][3][4][5][6][7]
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Contents
Community Commentary
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References
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- ↑ 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 SGD PMID 12023279
- ↑ 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 SGD PMID 8413229
- ↑ 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 SGD PMID 7500331
- ↑ 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 SGD PMID 12237310
- ↑ 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 SGD PMID 7628444
- ↑ Schmitt M, et al. (1996) The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria. J Cell Biol 134(6):1375-86 SGD PMID 8830768
- ↑ 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 SGD PMID 16460754
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