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Mitochondrial acyl carrier protein is involved in lipoic acid synthesis in Saccharomyces cerevisiae

The yeast gene, ACP1, encoding the mitochondrial acyl carrier protein, was deleted by gene replacement. The resulting acp1-deficient mutants had only 5–10% of the wild-type lipoic acid content remaining, and exhibited a respiratory-deficient phenotype. Upon meiosis, the lipoate deficiency co-segrega...

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Bibliographic Details
Published in:FEBS letters 1997-05, Vol.408 (2), p.217-220
Main Authors: Brody, Stuart, Oh, Changkyu, Hoja, Ursula, Schweizer, Eckhart
Format: Article
Language:English
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Summary:The yeast gene, ACP1, encoding the mitochondrial acyl carrier protein, was deleted by gene replacement. The resulting acp1-deficient mutants had only 5–10% of the wild-type lipoic acid content remaining, and exhibited a respiratory-deficient phenotype. Upon meiosis, the lipoate deficiency co-segregated with the acp1 deletion. The role of ACP1 in long-chain fatty acid synthesis was studied in fas1 and fas2 null mutants completely lacking cytoplasmic fatty acid synthase. When grown on odd-chain (13:0 and 15:0) fatty acids, these cells showed less than 1% of C-16 and C-18 acids in their total lipids. Mitochondrial ACP is therefore suggested to be involved with the biosynthesis of octanoate, a precurser to lipoic acid.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)00428-6