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Gene Review

HSP60  -  chaperone ATPase HSP60

Saccharomyces cerevisiae S288c

Synonyms: CPN60, Heat shock protein 60, mitochondrial, L8479.10, MIF4, MNA2, ...
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Disease relevance of HSP60


High impact information on HSP60

  • Our data argue against this model: import intermediates of cytochromes c1 and b2 were found only outside the inner membrane; maturation of these proteins was independent of the matrix-localized hsp60 chaperone; and dihydrofolate reductase linked to the presequence of either cytochrome was imported to the intermembrane space in the absence of ATP [3].
  • Heatshock protein 60 (hsp60) in the matrix of mitochondria is essential for the folding and assembly of newly imported proteins [4].
  • Hsp60 belongs to a class of structurally related chaperonins found in organelles of endosymbiotic origin and in the bacterial cytosol [4].
  • The hsp60 protein isolated from the protozoan Tetrahymena thermophila is induced in response to heat stress and is a member of an immunologically conserved family represented in Escherichia coli and in mitochondria of plants and animals [5].
  • In vitro, Hsp60 bound to DHFR in the course of thermal denaturation, preventing its aggregation, and mediated its adenosine triphosphate-dependent refolding at increased temperatures [2].

Biological context of HSP60

  • The HSP60 gene maps to chromosome XII [6].
  • The predicted HSP60 contains a mitochondrial target sequence and exhibits striking amino acid sequence similarity to its counterparts in bacteria, plants, and humans [7].
  • We have cloned the Saccharomyces cerevisiae HSP60 gene from a lambda gt11 genomic library using monoclonal antibodies, have obtained its sequence, determined its transcription start point, and shown that it exists as a single copy [7].
  • Heat shock protein HSP60 can alleviate the phenotype of mitochondrial RNA-deficient temperature-sensitive mna2 pet mutants [8].
  • Both mna2-1 and mna2-2, the two available alleles of mna2, have conservative single amino acid substitutions in the HSP60 gene [8].

Anatomical context of HSP60

  • HSP60 was found to be the genetic locus of the conditional-lethal mutation described by Cheng et al., which at non-permissive temperature is defective in the assembly of several different multisubunit complexes in mitochondria [5].
  • The recombinant HSP60 was used to immunize BALB/c mice and was shown to induce proliferation of T cells isolated from lymph nodes of these animals [9].
  • The mitochondrial heat shock protein 60 (Hsp60) has now been shown to form complexes with a variety of polypeptides in organelles exposed to heat stress [2].
  • Hsp60 subunits are encoded by a nuclear gene and translated in the cytosol as precursors which are translocated into mitochondria and proteolytically processed [4].
  • Electron and confocal microscopy revealed that hsp60 resided on the yeast cell wall in discrete clusters [10].

Associations of HSP60 with chemical compounds

  • When dimeric ribulose-1,5-bisphosphate carboxylase (Rubisco) is denatured and allowed to bind to yeast cpn60, subsequent refolding of Rubisco is strictly dependent upon yeast cpn10 [11].
  • Consistently, the iron chelator deferoxamine protected low Hsp60-expressing cells from both oxidant-induced death and protein oxidation [12].
  • We constructed mutant strains in which the levels of Hsp60 protein, compared with wild-type cells, were four times greater, and the addition of doxycycline gradually reduces them to 20% of wild-type [12].
  • As these enzymes release their iron ions under oxidative-stress conditions, the intracellular labile iron pool, monitored with calcein, was higher in cells with reduced Hsp60 levels [12].
  • Common targets include stress resistance proteins (Hsp60 and Hsp70) and enzymes involved in glucose metabolism such as enolase, glyceraldehydes-3-P dehydrogenase, fructose-1,6-biphosphate aldolase, pyruvate decarboxylase, and alcohol dehydrogenase [13].

Physical interactions of HSP60

  • In the presence of ADP, one molecule of hsp10 binds to hsp60 with an apparent Kd of 0.9 nM and a second molecule of hsp10 binds with a Kd of 24 nM [14].

Other interactions of HSP60

  • Our results identify Hsp10 as an essential component of the mitochondrial protein folding apparatus, participating in various aspects of Hsp60 function [1].
  • Depletion of Mrs5p in yeast cells causes accumulation of unprocessed precursors of the mitochondrial hsp60 protein and defects in all cytochrome complexes [15].
  • The Tcm62p sequence is 17.3% identical to yeast hsp60, a molecular chaperone [16].
  • One H. polymorpha 70 kDa protein was strongly induced during growth at elevated temperatures, whereas a second 70 kDa protein as well as a 60 kDa protein showed strong protein sequence homology to mitochondrial SSC1 and hsp60, respectively, from S. cerevisiae [17].
  • Depletion of Mrs11p results in a phenotype similar to that observed in Mrs5p-depleted cells: accumulation of the precursor form of mitochondrial hsp60, inability to form spectrophotometrically detectable amounts of cytochromes and changes in the mitochondrial morphology [18].

Analytical, diagnostic and therapeutic context of HSP60

  • mna2, which belongs to the class I temperature-sensitive pet mutants that lose mitochondrial (mt)RNA at restrictive temperature, was shown by complementation and sequence determination to correspond to the gene coding for HSP60 [8].
  • HSP60 expression appeared to be regulated during form transition in Pb, as different levels of expression were detected in in vitro labeling of cells and northern blot analysis [19].
  • In the presence of MgATP, yeast cpn60 and yeast cpn10 form a stable complex that can be isolated by gel filtration and that facilitates refolding of denatured Rubisco [11].
  • By electron microscopy, these particles are ring-shaped and reminiscent of proteins in the Hsp60 and TF55/TCP families [20].
  • Of the methods that we tested for monitoring the association of imported proteins with hsp60, only co-immunoprecipitation with specific anti-hsp60 antibodies proved to be reliable [21].


  1. Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. Höhfeld, J., Hartl, F.U. J. Cell Biol. (1994) [Pubmed]
  2. Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Martin, J., Horwich, A.L., Hartl, F.U. Science (1992) [Pubmed]
  3. Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism. Glick, B.S., Brandt, A., Cunningham, K., Müller, S., Hallberg, R.L., Schatz, G. Cell (1992) [Pubmed]
  4. The mitochondrial chaperonin hsp60 is required for its own assembly. Cheng, M.Y., Hartl, F.U., Horwich, A.L. Nature (1990) [Pubmed]
  5. Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Reading, D.S., Hallberg, R.L., Myers, A.M. Nature (1989) [Pubmed]
  6. The 66 kDa component of yeast SFI, stimulatory factor I, is hsp60. Smiley, J.K., Brown, W.C., Campbell, J.L. Nucleic Acids Res. (1992) [Pubmed]
  7. Cloning and characterization of the yeast chaperonin HSP60 gene. Johnson, R.B., Fearon, K., Mason, T., Jindal, S. Gene (1989) [Pubmed]
  8. Heat shock protein HSP60 can alleviate the phenotype of mitochondrial RNA-deficient temperature-sensitive mna2 pet mutants. Sanyal, A., Harington, A., Herbert, C.J., Groudinsky, O., Slonimski, P.P., Tung, B., Getz, G.S. Mol. Gen. Genet. (1995) [Pubmed]
  9. The hsp60 gene of the human pathogenic fungus Coccidioides immitis encodes a T-cell reactive protein. Thomas, P.W., Wyckoff, E.E., Pishko, E.J., Yu, J.J., Kirkland, T.N., Cole, G.T. Gene (1997) [Pubmed]
  10. Identification of heat shock protein 60 as the ligand on Histoplasma capsulatum that mediates binding to CD18 receptors on human macrophages. Long, K.H., Gomez, F.J., Morris, R.E., Newman, S.L. J. Immunol. (2003) [Pubmed]
  11. Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Rospert, S., Glick, B.S., Jenö, P., Schatz, G., Todd, M.J., Lorimer, G.H., Viitanen, P.V. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  12. Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae. Cabiscol, E., Bellí, G., Tamarit, J., Echave, P., Herrero, E., Ros, J. J. Biol. Chem. (2002) [Pubmed]
  13. Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction. Reverter-Branchat, G., Cabiscol, E., Tamarit, J., Ros, J. J. Biol. Chem. (2004) [Pubmed]
  14. Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60. Dubaquié, Y., Looser, R., Rospert, S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  15. Mrs5p, an essential protein of the mitochondrial intermembrane space, affects protein import into yeast mitochondria. Jarosch, E., Tuller, G., Daum, G., Waldherr, M., Voskova, A., Schweyen, R.J. J. Biol. Chem. (1996) [Pubmed]
  16. The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for the assembly of the mitochondrial succinate dehydrogenase (complex II). Dibrov, E., Fu, S., Lemire, B.D. J. Biol. Chem. (1998) [Pubmed]
  17. Affinity purification of molecular chaperones of the yeast Hansenula polymorpha using immobilized denatured alcohol oxidase. Evers, M.E., Huhse, B., Titorenko, V.I., Kunau, W.H., Hartl, F.U., Harder, W., Veenhuis, M. FEBS Lett. (1993) [Pubmed]
  18. A soluble 12-kDa protein of the mitochondrial intermembrane space, Mrs11p, is essential for mitochondrial biogenesis and viability of yeast cells. Jarosch, E., Rödel, G., Schweyen, R.J. Mol. Gen. Genet. (1997) [Pubmed]
  19. Molecular cloning, characterization and expression of the heat shock protein 60 gene from the human pathogenic fungus Paracoccidioides brasiliensis. Izacc, S.M., Gomez, F.J., Jesuino, R.S., Fonseca, C.A., Felipe, M.S., Deepe, G.S., Soares, C.M. Med. Mycol. (2001) [Pubmed]
  20. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. Parsell, D.A., Kowal, A.S., Lindquist, S. J. Biol. Chem. (1994) [Pubmed]
  21. Fusion proteins containing the cytochrome b2 presequence are sorted to the mitochondrial intermembrane space independently of hsp60. Rospert, S., Müller, S., Schatz, G., Glick, B.S. J. Biol. Chem. (1994) [Pubmed]
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