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Journal of Bacteriology, May 2007, p. 3635-3638, Vol. 189, No. 9
0021-9193/07/$08.00+0     doi:10.1128/JB.01757-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

In Vivo Modulation of a DnaJ Homolog, CbpA, by CbpM{triangledown}

Matthew R. Chenoweth,1 Nancy Trun,2 and Sue Wickner1*

Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892,1 Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 152822

Received 16 November 2006/ Accepted 19 February 2007

CbpA, an Escherichia coli DnaJ homolog, can function as a cochaperone for the DnaK/Hsp70 chaperone system, and its in vitro activity can be modulated by CbpM. We discovered that CbpM specifically inhibits the in vivo activity of CbpA, preventing it from functioning in cell growth and division. Furthermore, we have shown that CbpM interacts with CbpA in vivo during stationary phase, suggesting that the inhibition of activity is a result of the interaction. These results reveal that the activity of the E. coli DnaK system can be regulated in vivo by a specific inhibitor.

* Corresponding author. Mailing address: 37 Convent Dr., Rm 5144, Bethesda, MD 20892. Phone: (301) 496-2629. Fax: (301) 496-2212. E-mail: WicknerS{at}mail.nih.gov

{triangledown} Published ahead of print on 2 March 2007.

Journal of Bacteriology, May 2007, p. 3635-3638, Vol. 189, No. 9
0021-9193/07/$08.00+0     doi:10.1128/JB.01757-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chenoweth, M. R., Wickner, S. (2008). Complex Regulation of the DnaJ Homolog CbpA by the Global Regulators {sigma}S and Lrp, by the Specific Inhibitor CbpM, and by the Proteolytic Degradation of CbpM. J. Bacteriol. 190: 5153-5161 [Abstract] [Full Text]  


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