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• W1625133606 abstract "Abstract Earlier studies from this laboratory have shown that cytochrome c oxidase from bakers' yeast consists of seven polypeptides. The three largest ones (molecular weights 42,000, 34,500, and 23,000) are synthesized on mitochondrial ribosomes, whereas the four smallest ones (molecular weights 14,000, 12,500, 12,500, and 9,500) are synthesized on cytoplasmic ribosomes. In order to study the assembly of the functional oligomeric enzyme, four cytochrome c oxidase-less mutants of the Saccharomyces cerevisiae strain D273-10B were analyzed for residual cytochrome c oxidase polypeptides. Three were nuclear mutants specifically deficient in cytochrome c oxidase; the fourth mutant was an extrachromosomally inherited petite strain lacking not only cytochrome c oxidase but several other mitochondrial components as well. Cytochrome c oxidase polypeptides in the respiration-deficient mitochondria were identified by immunodiffusion and by electrophoretic analysis of radioactively labeled immunoprecipitates. Each of the three nuclear mutants lacked at least one cytochrome c oxidase component which, in the wild type, is synthesized on mitochondrial ribosomes. Mutant pet 494 was devoid of the 23,000-dalton polypeptide, whereas mutants pet E11 and pet 1030 were almost completely deficient in all three large cytochrome oxidase polypeptides. All nuclear mutants possessed near normal amounts of the cytoplasmically synthesized cytochrome c oxidase components. The extrachromosomal petite mutant lacked not only the three mitochondrially synthesized polypeptides, but also the 9,500-dalton polypeptide which is a product of cytoplasmic protein synthesis. The remaining cytochrome oxidase subunits were only loosely bound to the mitochondrial membrane, differing in this respect from the corresponding subunits in wild type mitochondria. These results permit the following conclusions. 1. The polypeptide of molecular weight 23,000 is apparently an essential component of cytochrome c oxidase, since its absence in mutant pet 494 is paralleled by a specific loss of the functional enzyme. 2. The mitochondrially synthesized cytochrome c oxidase subunits are necessary for the tight binding of the cytoplasmically synthesized cytochrome c oxidase subunits to the mitochondrial inner membrane. 3. The synthesis (or intregration) of mitochondrially synthesized cytochrome c oxidase subunits can be prevented by nuclear mutations. Conversely, extrachromosomal mutations can impair or completely prevent the integration of cytoplasmically synthesized cytochrome c oxidase subunits. These experiments also showed that, under our conditions, the three large subunits of cytochrome c oxidase account for 20 to 25% of the protein synthesized by mitochondria." @default.
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• W1625133606 date "1973-08-01" @default.
• W1625133606 modified "2023-10-16" @default.
• W1625133606 title "Mitochondrial Assembly in Respiration-deficient Mutants of Saccharomyces cerevisiae" @default.
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• W1625133606 doi "https://doi.org/10.1016/s0021-9258(19)43610-7" @default.
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