YDR258C
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| 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
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References
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- Jump up ↑ 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
- Jump up ↑ 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
- Jump up ↑ 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
- Jump up ↑ 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
- Jump up ↑ 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
- Jump up ↑ 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
- Jump up ↑ 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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