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Volume 270,
Number 49,
Issue of December 8, 1995 pp. 29096-29104
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Pleiotropic
Regulation of Central Carbohydrate Metabolism in Escherichia coli via the Gene csrA
(Received for publication, June 23, 1995; and in revised form, August 30, 1995)
Nirupama A.
Sabnis
,
Honghui
Yang
,
Tony
Romeo
The carbon storage regulator gene csrA has been shown
previously to dramatically affect the biosynthesis of intracellular
glycogen in Escherichia coli through its negative control of
the expression of two glycogen biosynthetic operons and the
gluconeogenic gene pckA (Romeo, T., Gong, M., Liu, M. Y., and
Brun-Zinkernagel, A. M.(1993) J. Bacteriol. 175,
4744-4755). Examination of the effects of csrA on
several enzymes, genes, and metabolites of central carbohydrate
metabolism now establishes a more extensive role for csrA in
directing intracellular carbon flux. Phosphoglucomutase and the
gluconeogenic enzymes fructose-1,6-bisphosphatase and
phosphoenolpyruvate synthetase were found to be under the negative
control of csrA, and these enzyme activities were maximal
during the early stationary phase of growth. The enzymes
glucose-6-phosphate isomerase, triose-phosphate isomerase, and enolase
were positively regulated by csrA. Thus, csrA exerts
reciprocal effects on glycolysis versus gluconeogenesis and
glycogen biosynthesis. The glycolytic isozymes pyruvate kinase F and A
(encoded by pykF and pykA, respectively) and
phosphofructokinase I and II (pfkA and pfkB,
respectively) exhibited differential regulation via csrA.
Since the individual members of these isozyme pairs are allosterically
regulated by different cellular metabolites, csrA is also
capable of fine-tuning the allosteric regulation of glycolysis. In
contrast, the expression of genes of the pentose phosphate pathway was
weakly or negligibly affected by csrA.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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