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. 1975 Jun;72(6):2054–2057. doi: 10.1073/pnas.72.6.2054

Properties of cytoplasmic mutants of Saccharomyces cerevisiae with specific lesions in cytochrome oxidase.

A Tzagoloff, A Akai, R B Needleman
PMCID: PMC432691  PMID: 166377

Abstract

Two mutants with specific defects in cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase; EC 1.9.3.1) have been isolated from cultures of Saccharomyces cerevisiae exposed to the mutagens ethyl-methane sulfonate and Mn++. The mutations have been shown to be extranuclear by two criteria. The phenotype persists in diploids formed by a cross with a p-o strain of yeast of the opposite mating type. Tetrad analysis indicates a non-Mendelian segregation (4:0 and 0:4) of the mutations. Both mutants show a total absence of cytochrome oxidase activity and of spectral cytochromes a and as. One of the mutants has been shown to be missing a polypeptide synthesized by mitochondria. The migration of this protein on polyacrylamide gels corresponds to the highest-molecular-weight subunit of cytochrome oxidase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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