TY  - JOUR
AU  - Jovanović, Goran
AU  - Engl, Christoph
AU  - Mayhew, Antony J.
AU  - Burrows, Patricia C.
AU  - Buck, Martin
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/437
AB  - The phage-shock-protein (Psp) response maintains the proton-motive force (pmf) under extracytoplasmic stress conditions that impair the inner membrane (IM) in bacterial cells. In Escherichia coli transcription of the pspABCDE and pspG genes requires activation of sigma(54)-RNA polymerase by the enhancer-binding protein PspF. A regulatory network comprising PspF-A -C-B-ArcB controls psp expression. One key regulatory point is the negative control of PspF imposed by its binding to PspA. It has been proposed that under stress conditions, the IM-bound sensors PspB and PspC receive and transduce the signal(s) to PspA via protein-protein interactions, resulting in the release of the PspA PspF inhibitory complex and the consequent induction of psp. In this work we demonstrate that PspB self-associates and interacts with PspC via putative IM regions. We present evidence suggesting that PspC has two topologies and that conserved residue G48 and the putative leucine zipper motif are determinants required for PspA interaction and signal transduction upon stress. We also establish that PspC directly interacts with the effector PspG, and show that PspG self-associates. These results are discussed in the context of formation and function of the Psp regulatory complex.
PB  - Microbiology Soc, London
T2  - Microbiology-Sgm
T1  - Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli
EP  - 2932
SP  - 2920
VL  - 156
DO  - 10.1099/mic.0.040055-0
ER  - 

@article{
author = "Jovanović, Goran and Engl, Christoph and Mayhew, Antony J. and Burrows, Patricia C. and Buck, Martin",
year = "2010",
abstract = "The phage-shock-protein (Psp) response maintains the proton-motive force (pmf) under extracytoplasmic stress conditions that impair the inner membrane (IM) in bacterial cells. In Escherichia coli transcription of the pspABCDE and pspG genes requires activation of sigma(54)-RNA polymerase by the enhancer-binding protein PspF. A regulatory network comprising PspF-A -C-B-ArcB controls psp expression. One key regulatory point is the negative control of PspF imposed by its binding to PspA. It has been proposed that under stress conditions, the IM-bound sensors PspB and PspC receive and transduce the signal(s) to PspA via protein-protein interactions, resulting in the release of the PspA PspF inhibitory complex and the consequent induction of psp. In this work we demonstrate that PspB self-associates and interacts with PspC via putative IM regions. We present evidence suggesting that PspC has two topologies and that conserved residue G48 and the putative leucine zipper motif are determinants required for PspA interaction and signal transduction upon stress. We also establish that PspC directly interacts with the effector PspG, and show that PspG self-associates. These results are discussed in the context of formation and function of the Psp regulatory complex.",
publisher = "Microbiology Soc, London",
journal = "Microbiology-Sgm",
title = "Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli",
pages = "2932-2920",
volume = "156",
doi = "10.1099/mic.0.040055-0"
}

Jovanović, G., Engl, C., Mayhew, A. J., Burrows, P. C.,& Buck, M.. (2010). Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli. in Microbiology-Sgm
Microbiology Soc, London., 156, 2920-2932.
https://doi.org/10.1099/mic.0.040055-0

Jovanović G, Engl C, Mayhew AJ, Burrows PC, Buck M. Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli. in Microbiology-Sgm. 2010;156:2920-2932.
doi:10.1099/mic.0.040055-0 .

Jovanović, Goran, Engl, Christoph, Mayhew, Antony J., Burrows, Patricia C., Buck, Martin, "Properties of the phage-shock-protein (Psp) regulatory complex that govern signal transduction and induction of the Psp response in Escherichia coli" in Microbiology-Sgm, 156 (2010):2920-2932,
https://doi.org/10.1099/mic.0.040055-0 . .

TY  - JOUR
AU  - Jovanović, Goran
AU  - Lloyd, Louise J.
AU  - Stumpf, Michael P. H.
AU  - Mayhew, Antony J.
AU  - Buck, Martin
PY  - 2006
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/239
AB  - 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.
PB  - Amer Soc Biochemistry Molecular Biology Inc, Bethesda
T2  - Journal of Biological Chemistry
T1  - Induction and function of the phage shock protein extracytoplasmic stress response in Escherichia coli
EP  - 21161
IS  - 30
SP  - 21147
VL  - 281
DO  - 10.1074/jbc.M602323200
ER  - 

@article{
author = "Jovanović, Goran and Lloyd, Louise J. and Stumpf, Michael P. H. and Mayhew, Antony J. and Buck, Martin",
year = "2006",
abstract = "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.",
publisher = "Amer Soc Biochemistry Molecular Biology Inc, Bethesda",
journal = "Journal of Biological Chemistry",
title = "Induction and function of the phage shock protein extracytoplasmic stress response in Escherichia coli",
pages = "21161-21147",
number = "30",
volume = "281",
doi = "10.1074/jbc.M602323200"
}

Jovanović, G., Lloyd, L. J., Stumpf, M. P. H., Mayhew, A. J.,& Buck, M.. (2006). Induction and function of the phage shock protein extracytoplasmic stress response in Escherichia coli. in Journal of Biological Chemistry
Amer Soc Biochemistry Molecular Biology Inc, Bethesda., 281(30), 21147-21161.
https://doi.org/10.1074/jbc.M602323200

Jovanović G, Lloyd LJ, Stumpf MPH, Mayhew AJ, Buck M. Induction and function of the phage shock protein extracytoplasmic stress response in Escherichia coli. in Journal of Biological Chemistry. 2006;281(30):21147-21161.
doi:10.1074/jbc.M602323200 .

Jovanović, Goran, Lloyd, Louise J., Stumpf, Michael P. H., Mayhew, Antony J., Buck, Martin, "Induction and function of the phage shock protein extracytoplasmic stress response in Escherichia coli" in Journal of Biological Chemistry, 281, no. 30 (2006):21147-21161,
https://doi.org/10.1074/jbc.M602323200 . .