title: Regulation of acetyl coenzyme A synthetase in Escherichia coli.
abstract: Cells of Escherichia coli growing on sugars that result in catabolite repression or amino acids that feed into glycolysis undergo a metabolic switch associated with the production and utilization of acetate. As they divide exponentially, these cells excrete acetate via the phosphotransacetylase-acetate kinase pathway. As they begin the transition to stationary phase, they instead resorb acetate, activate it to acetyl coenzyme A (acetyl-CoA) by means of the enzyme acetyl-CoA synthetase (Acs) and utilize it to generate energy and biosynthetic components via the tricarboxylic acid cycle and the glyoxylate shunt, respectively. Here, we present evidence that this switch occurs primarily through the induction of acs and that the timing and magnitude of this induction depend, in part, on the direct action of the carbon regulator cyclic AMP receptor protein (CRP) and the oxygen regulator FNR. It also depends, probably indirectly, upon the glyoxylate shunt repressor IclR, its activator FadR, and many enzymes involved in acetate metabolism. On the basis of these results, we propose that cells induce acs, and thus their ability to assimilate acetate, in response to rising cyclic AMP levels, falling oxygen partial pressure, and the flux of carbon through acetate-associated pathways.
authors.affiliation: Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois 60153, USA.
authors.forename: S
authors.initials: S
authors.lastname: Kumari
authors.forename: C M
authors.initials: CM
authors.lastname: Beatty
authors.forename: D F
authors.initials: DF
authors.lastname: Browning
authors.forename: S J
authors.initials: SJ
authors.lastname: Busby
authors.forename: E J
authors.initials: EJ
authors.lastname: Simel
authors.forename: G
authors.initials: G
authors.lastname: Hovel-Miner
authors.forename: A J
authors.initials: AJ
authors.lastname: Wolfe
mesh_terms: D000106:Acetate-CoA Ligase / Q000096:biosynthesis* / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D000242:Cyclic AMP / Q000378:metabolism; D002373:Cyclic AMP Receptor Protein / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D004790:Enzyme Induction; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D008956:Models, Chemical; D010100:Oxygen; D010313:Partial Pressure; D014157:Transcription Factors / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D001426:Bacterial Proteins; D002373:Cyclic AMP Receptor Protein; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C060704:FNR protein, E coli; D007506:Iron-Sulfur Proteins; D014157:Transcription Factors; D000242:Cyclic AMP; D000106:Acetate-CoA Ligase; D010100:Oxygen