YPL240C
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| Systematic name | YPL240C | |
| Gene name | HSP82 | |
| Aliases | HSP90 | |
| Feature type | ORF, Verified | |
| Coordinates | Chr XVI:98625..96496 | |
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Description of YPL240C: Cytoplasmic chaperone (Hsp90 family) required for pheromone signaling and negative regulation of Hsf1p; docks with the mitochondrial import receptor Tom70p for preprotein delivery; interacts with co-chaperones Cns1p, Cpr6p, Cpr7p, and Sti1p[1][2][3][4][5][6]
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Interactions
Physical
Physical interaction with cns1
Cns1 binds both to Hsp90 and to the yeast Hsp70 protein Ssa1 with comparable affinities. This is reminiscent of Sti1, another TPR-containing co-chaperone. [7] [8]
References
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- ↑ Young JC, et al. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112(1):41-50 SGD PMID 12526792
- ↑ Prodromou C, et al. (1999) Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 18(3):754-62 SGD PMID 9927435
- ↑ Louvion JF, et al. (1998) Hsp90 is required for pheromone signaling in yeast. Mol Biol Cell 9(11):3071-83 SGD PMID 9802897
- ↑ Duina AA, et al. (1998) Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. J Biol Chem 273(30):18974-8 SGD PMID 9668076
- ↑ Marsh JA, et al. (1998) Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells. Mol Cell Biol 18(12):7353-9 SGD PMID 9819422
- ↑ Dolinski KJ, et al. (1998) CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90. Mol Cell Biol 18(12):7344-52 SGD PMID 9819421
- ↑ Hainzl O, et al. (2004) Cns1 is an activator of the Ssa1 ATPase activity. J Biol Chem 279(22):23267-73 SGD PMID 15044454
- ↑ submitted by Dr. Harald Wegele on 2004-07-15
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