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Mitochondrial acyl carrier protein is involved in lipoic acid synthesis in Saccharomyces cerevisiae
Author(s) -
Brody Stuart,
Oh Changkyu,
Hoja Ursula,
Schweizer Eckhart
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00428-6
Subject(s) - acyl carrier protein , lipoic acid , biochemistry , saccharomyces cerevisiae , mutant , mitochondrion , yeast , biology , gene , respiratory chain , enzyme , fatty acid synthesis , fatty acid synthase , mitochondrial respiratory chain , biosynthesis , chemistry , microbiology and biotechnology , antioxidant
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.