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Nuclear respiration-deficient mutants of Saccharomyces
cerevisiae previously assigned to complementation group G93 lack
cytochromes a and a
The G93 mutants are
complemented by a nuclear gene, designated COX14. The product
of this gene is a low molecular mass protein of 7,960 Da. A gene fusion
expressing a biotinylated form of Cox14p complements cox14 mutants, indicating partial functional equivalence. The
biotinylated derivative has been helpful in localizing Cox14p to the
mitochondrial membrane and demonstrating that it is not a hitherto
unrecognized subunit of cytochrome oxidase, although it does appear to
be associated with a high molecular weight complex. This evidence,
combined with the assembly-arrested phenotype of cox14 mutants, indicates that Cox14p, like several other recently
described mitochondrial constituents, provides an important function at
some late stage of the cytochrome oxidase assembly pathway.
Volume 270,
Number 26,
Issue of June 30, pp. 15585-15590, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
and detectable
cytochrome oxidase activity. Other respiratory chain carriers and the
ATPase complex are present at near wild-type levels, indicating that
the mutations specifically affect cytochrome oxidase. Since synthesis
of the mitochondrially derived subunits 1, 2, and 3 of cytochrome
oxidase is normal, the defect cannot be related to transcription of the
endogenous genes or processing and translation of the corresponding
RNAs. The results of Western analysis of the cytochrome oxidase
subunits encoded in nuclear DNA also argues against an effect of the
mutations on expression of these constituents.
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