Reading D S, Hallberg R L, Myers A M
Department of Zoology, Iowa State University, Ames 50011.
Nature. 1989 Feb 16;337(6208):655-9. doi: 10.1038/337655a0.
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.
从嗜热四膜虫原生动物中分离出的hsp60蛋白是在热应激反应中被诱导产生的，它是一个在免疫学上保守的家族成员，在大肠杆菌以及植物和动物的线粒体中都有代表。我们在此报告一个核基因HSP60的克隆和特性分析，该基因编码来自酿酒酵母的hsp60同源物。核苷酸序列分析表明，酵母hsp60与大肠杆菌的groEL蛋白以及叶绿体的核酮糖-1,5-二磷酸羧化酶/加氧酶结合蛋白（RBP）相关。发现HSP60是Cheng等人描述的条件致死突变的遗传位点，在非允许温度下，它在线粒体中几种不同多亚基复合物的组装方面存在缺陷。这些数据与以下假设一致，即与groEL相关的蛋白作为辅助因子发挥进化上保守的功能，促进多聚体蛋白复合物单个亚基的折叠和/或缔合。
