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J. Bacteriol., Jul 1995, 3894-3896, Vol 177, No. 13
Copyright © 1995, American Society for Microbiology

A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli

C Ueguchi, T Shiozawa, M Kakeda, H Yamada and T Mizuno
Laboratory of Molecular Microbiology, School of Agriculture, Nagoya University, Japan.

The CbpA protein is an analog of the DnaJ molecular chaperone of Escherichia coli. To gain insight into the function of CbpA, we examined the nature of a cbpA null mutation with special reference to those of dnaK and dnaJ null mutations. In particular, the cbpA dnaJ double-null mutant was found to exhibit severe defects in cell growth, namely, a very narrow temperature range for growth, a defect in cell division, and susceptibility to killing by carbon starvation. These phenotypes are very similar to those reported for dnaK null mutants but not to those of dnaJ null mutants. Our results are best interpreted by assuming that CbpA is capable of compensating for DnaJ for cell growth and thus that the function(s) of CbpA is closely related to that of DnaJ.

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