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Journal of Bacteriology, March 1999, p. 1827-1830, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

CspA, CspB, and CspG, Major Cold Shock Proteins of Escherichia coli, Are Induced at Low Temperature under Conditions That Completely Block Protein Synthesis

Jean-Pierre Etchegaray and Masayori Inouye*

Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854

Received 3 November 1998/Accepted 15 January 1999

CspA, CspB, and CspG, the major cold shock proteins of Escherichia coli, are dramatically induced upon temperature downshift. In this report, we examined the effects of kanamycin and chloramphenicol, inhibitors of protein synthesis, on cold shock inducibility of these proteins. Cell growth was completely blocked at 37°C in the presence of kanamycin (100 µg/ml) or chloramphenicol (200 µg/ml). After 10 min of incubation with the antibiotics at 37°C, cells were cold shocked at 15°C and labeled with [35S]methionine at 30 min after the cold shock. Surprisingly, the synthesis of all these cold shock proteins was induced at a significantly high level virtually in the absence of synthesis of any other protein, indicating that the cold shock proteins are able to bypass the inhibitory effect of the antibiotics. Possible bypass mechanisms are discussed. The levels of cspA and cspB mRNAs for the first hour at 15°C were hardly affected in the absence of new protein synthesis caused either by antibiotics or by amino acid starvation.

* Corresponding author. Mailing address: Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854. Phone: (732) 235-4115 or (732) 235-4540. Fax: (732) 235-4559 or (732) 235-4783. E-mail: inouye{at}rwja.umdnj.edu.

Journal of Bacteriology, March 1999, p. 1827-1830, Vol. 181, No. 6
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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