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Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant.

ABSTRACT: We have cloned the human homolog of the Saccharomyces cerevisiae COX10 gene by functional complementation of a yeast cox10 null mutant. The 2.8-kb cDNA encoding the human heme A:farnesyltransferase codes for a 443-aa protein with high homology to the yeast and bacterial farnesylases. The human COX10 homolog, however, does not complement the mutation as efficiently as the yeast COX10 protein, likely due to the heterologous environment. PCR amplification and Southern analysis confirm the existence of a large mRNA for the human protein, with an unusually long 3' untranslated region. This clone can now be used to screen patients with inherited deficiencies in cytochrome oxidase in which the mutations remain unidentified and are likely to reside in a protein influencing the assembly of the enzyme.

SUBMITTER: Glerum DM

PROVIDER: S-EPMC44624 | biostudies-other | 1994 Aug

REPOSITORIES: biostudies-other

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Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant.

Glerum D M DM Tzagoloff A A

Proceedings of the National Academy of Sciences of the United States of America 19940801 18

We have cloned the human homolog of the Saccharomyces cerevisiae COX10 gene by functional complementation of a yeast cox10 null mutant. The 2.8-kb cDNA encoding the human heme A:farnesyltransferase codes for a 443-aa protein with high homology to the yeast and bacterial farnesylases. The human COX10 homolog, however, does not complement the mutation as efficiently as the yeast COX10 protein, likely due to the heterologous environment. PCR amplification and Southern analysis confirm the existence ...[more]

PMID: 8078902

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