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Journal of Bacteriology, November 1999, p. 6772-6778, Vol. 181, No. 21
Department of Microbiology and Molecular
Genetics, Harvard Medical School, Boston, Massachusetts 02115
Received 16 June 1999/Accepted 26 August 1999
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.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
The CpxRA Signal Transduction System of
Escherichia coli: Growth-Related Autoactivation and Control
of Unanticipated Target Operons
*
Corresponding author. Mailing address: Department of
Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Phone: (617) 432-1925. Fax: (617)
738-7446. E-mail: elin{at}hms.harvard.edu.
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