Difference between revisions of "YDR258C"
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| − | '''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=' | + | '''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| | + | {{SGDpaper|S000072044}} PMID 12237310</ref> |
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Revision as of 14:05, 31 March 2009
Share your knowledge...Edit this entry! <protect>
| Systematic name | YDR258C |
| Gene name | HSP78 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:974240..971805 |
| 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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References
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- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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