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J Bacteriol, February 1998, p. 831-839, Vol. 180, No. 4
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

CpxP, a Stress-Combative Member of the Cpx Regulon

Paul N. Danesedagger and Thomas J. Silhavy*

Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544

Received 8 September 1997/Accepted 6 December 1997

The CpxA/R two-component signal transduction system of Escherichia coli can combat a variety of extracytoplasmic protein-mediated toxicities. The Cpx system performs this function, in part, by increasing the synthesis of the periplasmic protease, DegP. However, other factors are also employed by the Cpx system for this stress-combative function. In an effort to identify these remaining factors, we screened a collection of random lacZ operon fusions for those fusions whose transcription is regulated by CpxA/R. Through this approach, we have identified a new locus, cpxP, whose transcription is stimulated by activation of the Cpx pathway. cpxP specifies a periplasmic protein that can combat the lethal phenotype associated with the synthesis of a toxic envelope protein. In addition, we show that cpxP transcription is strongly induced by alkaline pH in a CpxA-dependent manner and that cpxP and cpx mutant strains display hypersensitivity to growth in alkaline conditions.

* Corresponding author. Mailing address: Department of Molecular Biology, Princeton University, Princeton, NJ 08544. Phone: (609) 258-5899. Fax: (609) 258-2769. E-mail: tsilhavy{at}molecular.princeton.edu.

dagger Present address: Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138.




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