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Journal of Bacteriology, October 2006, p. 6780-6785, Vol. 188, No. 19
0021-9193/06/$08.00+0 doi:10.1128/JB.00471-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Molecular Biology Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400085, India
Received 4 April 2006/ Accepted 20 July 2006
The CspA family of cold shock genes in Escherichia coli K-12 includes nine paralogs, cspA to cspI. Some of them have been implicated in cold stress adaptation. Screening for mutations among common laboratory E. coli strains showed a high degree of genetic diversity in cspC but not in cspA and cspE. This diversity in cspC was due to a wide spectrum of variations including insertions of IS elements, deletion, and point mutation. Northern analysis of these mutants showed loss of cspC expression in all but one case. Further analysis of the loss-of-function cspC mutants showed that they have a fitness advantage in broth culture after 24 h over their isogenic wild-type derivatives. Conversely, introduction of mutated cspC alleles conferred a competitive fitness advantage to AB1157, a commonly used laboratory strain. This provides the evidence that loss of cspC expression is both necessary and sufficient to confer a gain of fitness as seen in broth culture over 24 h. Together, these results ascribe a novel role in cellular growth at 37°C for CspC, a member of the cold shock domain-containing protein family.
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