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J. Biol. Chem., Vol. 279, Issue 53, 55707-55714, December 31, 2004
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**
From the
Department of Biological Sciences, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom, the ¶Department of Plant and Microbial Biology, University of California, Berkeley, California 94720-3102, and the ||Molecular Microbiology Group, Institute of Food Research, Norwich Research Park, Colney, Norwich NR4 7UA, United Kingdom
The phage shock protein operon (pspABCDE) of Escherichia coli is strongly up-regulated in response to overexpression of the filamentous phage secretin protein IV (pIV) and by many other stress conditions including defects in protein export. PspA has an established role in maintenance of the proton-motive force of the cell under stress conditions. Here we present evidence for a new member of the phage shock response in E. coli. Using transcriptional profiling, we show that the synthesis of pIV in E. coli leads to a highly restricted response limited to the up-regulation of the psp operon genes and yjbO. The psp operon and yjbO are also up-regulated in response to pIV in Salmonella enterica serovar Typhimurium. yjbO is a highly conserved gene found exclusively in bacteria that contain a psp operon but is physically unlinked to the psp operon. yjbO encodes a putative inner membrane protein that is co-controlled with the psp operon genes and is predicted to be an effector of the psp response in E. coli. We present evidence that yjbO expression is driven by
54-RNA polymerase, activated by PspF and integration host factor, and negatively regulated by PspA. PspF specifically regulates only members of the PspF regulon: pspABCDE and yjbO. We found that increased expression of YjbO results in decreased motility of bacteria. Because yjbO is co-conserved and co-regulated with the psp operon and is a member of the phage shock protein F regulon, we propose that yjbO be renamed pspG.
Received for publication, August 6, 2004 , and in revised form, October 5, 2004.
* This work was supported by The Wellcome Trust, a Biotechnology and Biological Sciences Research Council Core Strategic grant, and National Institutes of Health Grant GM38361 (to S. Kustu). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains Supplemental Tables I-III and Fig. S1.
Present address: Nature Reviews Journals, Porters South, 4 Crinan St., London N1 9XW, United Kingdom.
** To whom correspondence should be addressed. Tel.: 44-020-7594-5442; Fax: 44-020-7594-5419; E-mail: m.buck{at}imperial.ac.uk.
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