HSP60/YLR259C Literature Guide Help

Other names published for HSP60: CPN60, MIF4, MNA2, chaperone ATPase HSP60, YLR259C

HSP60 - Function/Process (24)

ReferenceOther Genes Addressed
Banci L, et al.  (2011) Copper exposure effects on yeast mitochondrial proteome. J Proteomics 74(11):2522-35
Bender T, et al.  (2011) Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease. Mol Biol Cell 22(5):541-54
Walter GM, et al.  (2011) Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes. J Biol Chem 286(47):40486-93
Rossignol T, et al.  (2009) The proteome of a wine yeast strain during fermentation, correlation with the transcriptome. J Appl Microbiol 107(1):47-55
Kaufman BA, et al.  (2003) A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae. J Cell Biol 163(3):457-61
Cabiscol E, et al.  (2002) Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae. J Biol Chem 277(46):44531-8
Fang YC and Cheng M  (2002) The effect of C-terminal mutations of HSP60 on protein folding. J Biomed Sci 9(3):223-33
Voos W and Rottgers K  (2002) Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim Biophys Acta 1592(1):51-62
Parissi V, et al.  (2001) Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60. J Virol 75(23):11344-53
Cabiscol E, et al.  (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem 275(35):27393-8
Kaufman BA, et al.  (2000) In organello formaldehyde crosslinking of proteins to mtDNA: identification of bifunctional proteins. Proc Natl Acad Sci U S A 97(14):7772-7
Dubaquie Y, et al.  (1998) Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. EMBO J 17(20):5868-76
Heyrovska N, et al.  (1998) Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding. Biol Chem 379(3):301-9
Dubaquie Y, et al.  (1997) Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Proc Natl Acad Sci U S A 94(17):9011-6
Rospert S, et al.  (1994) Fusion proteins containing the cytochrome b2 presequence are sorted to the mitochondrial intermembrane space independently of hsp60. J Biol Chem 269(25):17279-88
Hallberg EM, et al.  (1993) Loss of mitochondrial hsp60 function: nonequivalent effects on matrix-targeted and intermembrane-targeted proteins. Mol Cell Biol 13(5):3050-7
Miller BR and Cumsky MG  (1993) Intramitochondrial sorting of the precursor to yeast cytochrome c oxidase subunit Va. J Cell Biol 121(5):1021-9
Glick BS, et al.  (1992) Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Cell 69(5):809-22
Koll H, et al.  (1992) Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68(6):1163-75
Martin J, et al.  (1992) Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science 258(5084):995-8
Cheng MY, et al.  (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348(6300):455-8
Cheng MY, et al.  (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337(6208):620-5
Reading DS, et al.  (1989) Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337(6208):655-9
Mueller DM, et al.  (1987) Temperature sensitive pet mutants in yeast Saccharomyces cerevisiae that lose mitochondrial RNA. Curr Genet 11(5):359-67