Affiliation:
1. Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115
Abstract
ABSTRACT
In
Escherichia coli
, the CpxRA two-component signal transduction system senses and responds to aggregated and misfolded proteins in the bacterial envelope. We show that CpxR-P (the phosphorylated form of the cognate response regulator) activates
cpxRA
expression in conjunction with RpoS, suggesting an involvement of the Cpx system in stationary-phase survival. Engagement of the CpxRA system in functions beyond protein management is indicated by several putative targets identified after a genomic screening for the CpxR-P recognition consensus sequence. Direct negative control of the newly identified targets
motABcheAW
(specifying motility and chemotaxis) and
tsr
(encoding the serine chemoreceptor) by CpxR-P was shown by electrophoretic mobility shift analysis and Northern hybridization. The results suggest that the CpxRA system plays a core role in an extensive stress response network in which the coordination of protein turnover and energy conservation may be the unifying element.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
126 articles.
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