Abstract:
: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 fast 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 precursor to lipoic acid.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Brody S,Oh C,Hoja U,Schweizer Edoi
10.1016/s0014-5793(97)00428-6subject
Has Abstractpub_date
1997-05-19 00:00:00pages
217-20issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00428-6journal_volume
408pub_type
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