Modifications of the relative proteolipid composition in the ATP synthase of a respiratory competent mutant of Saccharomyces cerevisiae.

A comparative study of the proteolipid composition of the F0-sector of the ATP synthase of wild-type strain of Saccharomyces cerevisiae and of nuclear mutants, modified at the level of the oxidative phosphorylation due to an enhanced proton permeability of the inner membrane, was carried out. Analysis of the crude proteolipid extract by electrophoresis and high liquid performance chromatography showed some differences at the level of mitochondrial DNA encoded proteolipids. Subunit 6 and in particular subunit 8 were present in reduced amounts, whereas subunit 9 was present in equal amounts in both types of strain. However, the phosphate binding affinity of subunit 8 was the same in wild-type and mutant strains. The fact that subunit 6 and subunit 8 are cotranscripted on a single mRNA led to the problem of the regulation of the mitochondrial synthesis of these two proteins by a nuclear gene.