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J. Biol. Chem., Vol. 260, Issue 10, 5871-5874, May, 1985
TJ Koerner, G Homison and A Tzagoloff
A collection of pet mutants of Saccharomyces cerevisiae has been screened
for lesions in cytochrome oxidase. Three different complementation groups
have been identified to consist of strains with altered forms of subunits
4, 5, or 6 that are known to be encoded by nuclear genes. The mutant
proteins cross-react with antiserum to the holoenzyme or to the individual
subunits but exhibit either an increase or decrease in size. In each
instance the mutation imparts a respiratory deficient phenotype which is
due to reduced levels of cytochrome oxidase activity in the mitochondria.
These results indicate that each of the three proteins is required either
for the catalytic activity or for the assembly of functional cytochrome
oxidase.
Nuclear mutants of Saccharomyces cerevisiae with altered subunits 4, 5, and 6 of cytochrome oxidase
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