Induction and function of the phage shock protein extracytoplasmic stress response in Escherichia coli.
The phage shock protein (Psp) F regulon response in Escherichia coli is thought to be induced by impaired inner membrane integrity and an associated decrease in proton motive force (pmf). Mechanisms by which the Psp system detects the stress signal and responds have so far remained undetermined. Here we demonstrate that PspA and PspG directly confront a variety of inducing stimuli by switching the cell to anaerobic respiration and fermentation and by down-regulating motility, thereby subtly adjusting and maintaining energy usage and pmf. Additionally, PspG controls iron usage. We show that the Psp-inducing protein IV secretin stress, in the absence of Psp proteins, decreases the pmf in an ArcB-dependent manner and that ArcB is required for amplifying and transducing the stress signal to the PspF regulon. The requirement of the ArcB signal transduction protein for induction of psp provides clear evidence for a direct link between the physiological redox state of the cell, the electron transport chain, and induction of the Psp response. Under normal growth conditions PspA and PspD control the level of activity of ArcB/ArcA system that senses the redox/metabolic state of the cell, whereas under stress conditions PspA, PspD, and PspG deliver their effector functions at least in part by activating ArcB/ArcA through positive feedback.
Jovanovic
Goran
G
Division of Biology, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Lloyd
Louise J
LJ
Division of Biology, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Stumpf
Michael P H
MPH
Centre for Bioinformatics, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Mayhew
Antony J
AJ
Division of Biology, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
Buck
Martin
M
Division of Biology, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom. Electronic address: m.buck@imperial.ac.uk.
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001435:Bacteriophages / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism* / Q000502:physiology*; D015964:Gene Expression Regulation, Bacterial; D006360:Heat-Shock Proteins / Q000378:metabolism*; D008564:Membrane Potentials; D008565:Membrane Proteins / Q000378:metabolism*; D018613:Microscopy, Confocal; D010084:Oxidation-Reduction; D010957:Plasmids / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D012097:Repressor Proteins / Q000378:metabolism; D012633:Secretin / Q000378:metabolism; D015534:Trans-Activators / Q000378:metabolism / Q000502:physiology*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D008565:Membrane Proteins; C513446:PspD protein, E coli; C098954:PspF protein, E coli; D012097:Repressor Proteins; D015534:Trans-Activators; C041610:arcA protein, E coli; C496547:phage shock protein G, E coli; C069816:phage shock protein, Bacteria; D012633:Secretin; D011494:Protein Kinases; C065271:arcB protein, E coli