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Papers In Press, published online ahead of print October 13, 2004
Biological Science, Imperial College London, London SW7 2AZ
Corresponding Author: l.lloyd{at}ic.ac.uk
The phage shock protein operon (pspABCDE) of Escherichia coli is strongly upregulated in response to over-expression 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 upregulation 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 which 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 sigma54-RNA polymerase, activated by PspF and IHF, 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. Since 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.
J. Biol. Chem, 10.1074/jbc.M408994200
Submitted on August 6, 2004
Revised on October 5, 2004
Accepted on October 13, 2004
Identification of a new member of the phage shock protein response in Escherichia coli, the phage shock protein G (PspG)
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