Cloning of a human gene involved in cytochrome oxidase assembly by functional complementation of an oxa1-mutation in Saccharomyces cerevisiae.
N Bonnefoy, M Kermorgant… - Proceedings of the …, 1994 - National Acad Sciences
N Bonnefoy, M Kermorgant, O Groudinsky, M Minet, PP Slonimski, G Dujardin
Proceedings of the National Academy of Sciences, 1994•National Acad SciencesThe yeast nuclear gene OXA1 is essential for cytochrome oxidase assembly, so that a null
mutation in the OXA1 gene leads to complete respiratory deficiency. We have cloned by
genetic selection a human OXA1 (OXA1Hs) cDNA that complements the respiratory defect of
yeast oxa1 mutants. The deduced sequence of the human protein shares 33% identity with
the yeast OXA1 protein. The OXA1Hs cDNA corresponds to a single and relatively highly
expressed gene. Oxygen consumption measurements and cytochrome absorption spectra …
mutation in the OXA1 gene leads to complete respiratory deficiency. We have cloned by
genetic selection a human OXA1 (OXA1Hs) cDNA that complements the respiratory defect of
yeast oxa1 mutants. The deduced sequence of the human protein shares 33% identity with
the yeast OXA1 protein. The OXA1Hs cDNA corresponds to a single and relatively highly
expressed gene. Oxygen consumption measurements and cytochrome absorption spectra …
The yeast nuclear gene OXA1 is essential for cytochrome oxidase assembly, so that a null mutation in the OXA1 gene leads to complete respiratory deficiency. We have cloned by genetic selection a human OXA1 (OXA1Hs) cDNA that complements the respiratory defect of yeast oxa1 mutants. The deduced sequence of the human protein shares 33% identity with the yeast OXA1 protein. The OXA1Hs cDNA corresponds to a single and relatively highly expressed gene. Oxygen consumption measurements and cytochrome absorption spectra show that replacement of the yeast protein with the human homolog leads to the correct assembly of cytochrome oxidase, suggesting that the proteins play essentially the same role in both organisms.
National Acad Sciences
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