Abstract
Acyl carrier protein (ACP) is modified on serine 36 by the covalent posttranslational attachment of 4'-phosphopantetheine from coenzyme A (CoA), and this modification is required for lipid biosynthesis. Jackowski and Rock (J. Biol. Chem 258:15186-15191, 1983) reported that upon depletion of the CoA pool by starvation for a CoA precursor, no accumulation of the unmodified form of ACP (apo-ACP) was detected. We report that this lack of apo-ACP accumulation results from decreased translation of the acpP mRNAs because of the limitation of the synthesis of glutamate and other amino acids made directly from tricarboxylic acid cycle intermediates.
Original language | English (US) |
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Pages (from-to) | 2662-2667 |
Number of pages | 6 |
Journal | Journal of bacteriology |
Volume | 178 |
Issue number | 9 |
DOIs | |
State | Published - May 1996 |
ASJC Scopus subject areas
- Microbiology
- Molecular Biology