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Journal of Bacteriology, August 1998, p. 4287-4290, Vol. 180, No. 16
Department of Microbiology and Immunology,
Stanford University School of Medicine, Stanford, California 94305
Received 14 January 1998/Accepted 3 June 1998
Escherichia coli strains mutant in the starvation gene
cstC grow normally in a mineral salts medium but are
impaired in utilizing amino acids as nitrogen sources. They are also
compromised in starvation survival, where amino acid catabolism is
important. The cstC gene encodes a 406-amino-acid protein
that closely resembles the E. coli ArgD protein, which is
involved in arginine biosynthesis. We postulate that CstC is a
counterpart of ArgD in an amino acid catabolic pathway. The
cstC upstream region contains several regulatory consensus
sequences. Both
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The Escherichia coli Starvation Gene
cstC Is Involved in Amino Acid Catabolism


S and
54 promoters are
probably involved in cstC transcription and appear to
compete with each other, presumably to match cstC
expression to the cellular amino acid catabolic needs.
*
Corresponding author. Mailing address: D317 Sherman
Fairchild Science Building, Department of Microbiology & Immunology,
Stanford University School of Medicine, Stanford, CA 94305-5402. Phone: (650) 725-4745. Fax: (650) 725-6757. E-mail:
a.matin{at}forsythe.stanford.edu.
Present address: Department of Biochemistry, Stanford University
School of Medicine, Stanford, CA 94305-5307.
Present address: Department of Food Science & Technology, College
of Agriculture, Gyeongsang National University, Chinju, Korea 660-701.
§
Department of Biology, St. Joseph's University, Philadelphia, PA
19131.
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