Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor.
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. 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. coli and the RUBISCO-binding protein (RBP) of chloroplasts. 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. 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 complexes.
Reading
D S
DS
Department of Zoology, Iowa State University, Ames 50011.
Hallberg
R L
RL
Myers
A M
AM
D000595:Amino Acid Sequence; D001483:Base Sequence; D018834:Chaperonin 60; D005796:Genes; D005800:Genes, Fungal; D006360:Heat-Shock Proteins / Q000235:genetics*; D015151:Immunoblotting; D008928:Mitochondria / Q000378:metabolism*; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid
D018834:Chaperonin 60; D006360:Heat-Shock Proteins