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  - Joly, Nicolas
AU  - Burrows, Patricia C.
AU  - Engl, Christoph
AU  - Jovanović, Goran
AU  - Buck, Martin
PY  - 2009
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/369
AB  - To survive and colonise their various environments, including those used during infection, bacteria have developed a variety of adaptive systems. Amongst these is phage shock protein (Psp) response, which can be induced in Escherichia coli upon filamentous phage infection (specifically phage secretin pIV) and by other membrane-damaging agents. The E. coli Psp system comprises seven proteins, of which PspA is the central component. PspA is a bifunctional protein that is directly involved in (i) the negative regulation of the psp-specific transcriptional activator PspF and (ii) the maintenance of membrane integrity in a mechanism proposed to involve the formation of a 36-mer ring complex. Here we established that the PspA negative regulation of PspF ATPase activity is the result of a cooperative inhibition. We present biochemical evidence showing that an inhibitory PspA-PspF regulatory complex, which has significantly reduced PspF ATPase activity, is composed of around six PspF subunits and six PspA subunits, suggesting that PspA exists in at least two different oligomeric assemblies. We now establish that all four putative helical domains of PspA are critical for the formation of the 36-mer. In contrast, not all four helical domains are required for the formation of the inhibitory PspA-PspF complex. Since a range of initial PspF oligomeric states permit formation of the apparent PspA-PspF dodecameric assembly, we conclude that PspA and PspF demonstrate a strong propensity to self-assemble into a single defined heteromeric regulatory complex.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Molecular Biology
T1  - A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation
EP  - 775
IS  - 4
SP  - 764
VL  - 394
DO  - 10.1016/j.jmb.2009.09.055
ER  - 

@article{
author = "Joly, Nicolas and Burrows, Patricia C. and Engl, Christoph and Jovanović, Goran and Buck, Martin",
year = "2009",
abstract = "To survive and colonise their various environments, including those used during infection, bacteria have developed a variety of adaptive systems. Amongst these is phage shock protein (Psp) response, which can be induced in Escherichia coli upon filamentous phage infection (specifically phage secretin pIV) and by other membrane-damaging agents. The E. coli Psp system comprises seven proteins, of which PspA is the central component. PspA is a bifunctional protein that is directly involved in (i) the negative regulation of the psp-specific transcriptional activator PspF and (ii) the maintenance of membrane integrity in a mechanism proposed to involve the formation of a 36-mer ring complex. Here we established that the PspA negative regulation of PspF ATPase activity is the result of a cooperative inhibition. We present biochemical evidence showing that an inhibitory PspA-PspF regulatory complex, which has significantly reduced PspF ATPase activity, is composed of around six PspF subunits and six PspA subunits, suggesting that PspA exists in at least two different oligomeric assemblies. We now establish that all four putative helical domains of PspA are critical for the formation of the 36-mer. In contrast, not all four helical domains are required for the formation of the inhibitory PspA-PspF complex. Since a range of initial PspF oligomeric states permit formation of the apparent PspA-PspF dodecameric assembly, we conclude that PspA and PspF demonstrate a strong propensity to self-assemble into a single defined heteromeric regulatory complex.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Molecular Biology",
title = "A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation",
pages = "775-764",
number = "4",
volume = "394",
doi = "10.1016/j.jmb.2009.09.055"
}

Joly, N., Burrows, P. C., Engl, C., Jovanović, G.,& Buck, M.. (2009). A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation. in Journal of Molecular Biology
Academic Press Ltd- Elsevier Science Ltd, London., 394(4), 764-775.
https://doi.org/10.1016/j.jmb.2009.09.055

Joly N, Burrows PC, Engl C, Jovanović G, Buck M. A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation. in Journal of Molecular Biology. 2009;394(4):764-775.
doi:10.1016/j.jmb.2009.09.055 .

Joly, Nicolas, Burrows, Patricia C., Engl, Christoph, Jovanović, Goran, Buck, Martin, "A Lower-Order Oligomer Form of Phage Shock Protein A (PspA) Stably Associates with the Hexameric AAA(+) Transcription Activator Protein PspF for Negative Regulation" in Journal of Molecular Biology, 394, no. 4 (2009):764-775,
https://doi.org/10.1016/j.jmb.2009.09.055 . .