Abstract
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 animals1,2. We report here the cloning and characterization of a nuclear gene, HSP60, which codes for the hsp60 homologue from the yeast Saccharomyces cerevisiae. Nucleotide sequence analysis revealed that yeast hsp60 is related to the groEL protein of E. coli3-6 and the RUBISCO-binding protein (RBP) of chloroplasts7. HSP60 was found to be the genetic locus of the conditional-lethal mutation described by Cheng et al.8, which at non-permissive temperature is defective in the assembly of several different multisubunit complexes in mitochondria. These data are consistent with the hypothesis that the groEL-related proteins serve an evolutionarily conserved function as accessory factors facilitating the folding and/or association of individual subunits of multimeric protein complexes7,9-14.
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Reading, D., Hallberg, R. & Myers, A. Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337, 655–659 (1989). https://doi.org/10.1038/337655a0
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DOI: https://doi.org/10.1038/337655a0
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