The apparent coupling between synthesis and posttranslational modification of Escherichia coli acyl carrier protein is due to inhibition of amino acid biosynthesis

David H. Keating, Yan Zhang, John E. Cronan

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)2662-2667
Number of pages6
JournalJournal of bacteriology
Volume178
Issue number9
DOIs
StatePublished - May 1996

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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