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Journal of Bacteriology, August 2000, p. 4173-4179, Vol. 182, No. 15
Department of Microbiology and Immunology,
Stritch School of Medicine, Loyola University Chicago, Maywood,
Illinois 60153,1 and School of
Biosciences, The University of Birmingham, Birmingham B15 2TT, United
Kingdom2
Received 7 January 2000/Accepted 8 May 2000
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.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Regulation of Acetyl Coenzyme A Synthetase in
Escherichia coli

*
Corresponding author. Mailing address: Department of
Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Ave., Maguire Building 105, Rm. 3822, Maywood, IL 60153. Phone: (708) 216-5814. Fax: (708) 216-9574. E-mail:
awolfe{at}luc.edu.
Present address: Department of Oral Medicine and Diagnostic
Sciences, Harvard School of Dental Medicine, Boston, MA 02115.
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