This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Buelow, D. R.
Right arrow Articles by Raivio, T. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Buelow, D. R.
Right arrow Articles by Raivio, T. L.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2005, p. 6622-6630, Vol. 187, No. 19
0021-9193/05/$08.00+0     doi:10.1128/JB.187.19.6622-6630.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Cpx Signal Transduction Is Influenced by a Conserved N-Terminal Domain in the Novel Inhibitor CpxP and the Periplasmic Protease DegP

Daelynn R. Buelow and Tracy L. Raivio*

Department of Biological Sciences, University of Alberta, Edmonton, Alberta T6G 2E9, Canada

Received 2 May 2005/ Accepted 11 July 2005

In Escherichia coli, envelope stress can be overcome by three different envelope stress responses: the {sigma}E stress response and the Bae and Cpx two-component systems. The Cpx envelope stress response is controlled by the sensor kinase CpxA, the response regulator CpxR, and the novel periplasmic protein CpxP. CpxP mediates feedback inhibition of the Cpx pathway through a hypothetical interaction with the sensing domain of CpxA. No informative homologues of CpxP are known, and thus it is unclear how CpxP exerts this inhibition. Here, we identified six cpxP loss-of-function mutations using a CpxP-ß-lactamase (CpxP'-'Bla) translational fusion construct. These loss-of-function mutations identified a highly conserved, predicted {alpha}-helix in the N-terminal domain of CpxP that affects both the function and the stability of the protein. In the course of this study, we also found that CpxP'-'Bla stability is differentially controlled by the periplasmic protease DegP in response to inducing cues and that mutation of degP diminishes Cpx pathway activity. We propose that the N-terminal {alpha}-helix is an important functional domain for inhibition of the Cpx pathway and that CpxP is subject to DegP-dependent proteolysis.


* Corresponding author. Mailing address: Department of Biological Sciences, University of Alberta, Edmonton, Alberta T6G 2E9, Canada. Phone: (780) 492-3491. Fax: (780) 492-9234. E-mail: traivio{at}ualberta.ca.


Journal of Bacteriology, October 2005, p. 6622-6630, Vol. 187, No. 19
0021-9193/05/$08.00+0     doi:10.1128/JB.187.19.6622-6630.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Price, N. L., Raivio, T. L. (2009). Characterization of the Cpx Regulon in Escherichia coli Strain MC4100. J. Bacteriol. 191: 1798-1815 [Abstract] [Full Text]  
  • Wolfe, A. J., Parikh, N., Lima, B. P., Zemaitaitis, B. (2008). Signal Integration by the Two-Component Signal Transduction Response Regulator CpxR. J. Bacteriol. 190: 2314-2322 [Abstract] [Full Text]  
  • MacRitchie, D. M., Ward, J. D., Nevesinjac, A. Z., Raivio, T. L. (2008). Activation of the Cpx Envelope Stress Response Down-Regulates Expression of Several Locus of Enterocyte Effacement-Encoded Genes in Enteropathogenic Escherichia coli. Infect. Immun. 76: 1465-1475 [Abstract] [Full Text]  
  • Fleischer, R., Heermann, R., Jung, K., Hunke, S. (2007). Purification, Reconstitution, and Characterization of the CpxRAP Envelope Stress System of Escherichia coli. J. Biol. Chem. 282: 8583-8593 [Abstract] [Full Text]  
  • Hutchings, M. I., Hong, H.-J., Leibovitz, E., Sutcliffe, I. C., Buttner, M. J. (2006). The {sigma}E Cell Envelope Stress Response of Streptomyces coelicolor Is Influenced by a Novel Lipoprotein, CseA.. J. Bacteriol. 188: 7222-7229 [Abstract] [Full Text]