TY  - JOUR
AU  - Jovanović, Goran
AU  - Mehta, Parul
AU  - McDonald, Christopher
AU  - Davidson, Anthony C.
AU  - Uzdavinys, Povilas
AU  - Ying, Liming
AU  - Buck, Martin
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/782
AB  - The phage shock protein (Psp) systems found in bacteria, archaea and higher plants respond to extracytoplasmic stresses that damage the cytoplasmic membrane and enable cells to repair their membranes. The conserved membrane-associated effector protein PspA has four a-helical domains (HD1- HD4) and helps to repair the membrane as a high-order oligomer. In enterobacteria, under non-stress conditions, PspA as a low-order assembly directly inhibits its cognate transcription activator PspF. Here we show that N-terminal amphipathic helices ahA and ahB in PspA HD1 are functional determinants involved in negative gene control and stress signal perception and its transduction via interactions with the PspBC membrane stress sensors and the inner membrane (IM). The amphipathic helices enable PspA to switch from a low-order gene regulator into an IM-bound high-order effector complex under membrane stress. Conserved residue proline 25 is involved in sequential use of the amphipathic helices and ahA IM interaction. Single molecule imaging of eGFP-PspA and its amphipathic helices variants in live Escherichia coli cells show distinct spatial and temporal organisations of PspA corresponding to its negative control and effector functions. These findings inform studies on the role of the Psp system in persister cell formation and cell envelope protection in bacterial pathogens and provide a basis for exploring the specialised roles of PspA homologues such as YjfJ, LiaH and Vipp1.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Molecular Biology
T1  - The N-Terminal Amphipathic Helices Determine Regulatory and Effector Functions of Phage Shock Protein A (PspA) in Escherichia coli
EP  - 1511
IS  - 7
SP  - 1498
VL  - 426
DO  - 10.1016/j.jmb.2013.12.016
ER  - 

@article{
author = "Jovanović, Goran and Mehta, Parul and McDonald, Christopher and Davidson, Anthony C. and Uzdavinys, Povilas and Ying, Liming and Buck, Martin",
year = "2014",
abstract = "The phage shock protein (Psp) systems found in bacteria, archaea and higher plants respond to extracytoplasmic stresses that damage the cytoplasmic membrane and enable cells to repair their membranes. The conserved membrane-associated effector protein PspA has four a-helical domains (HD1- HD4) and helps to repair the membrane as a high-order oligomer. In enterobacteria, under non-stress conditions, PspA as a low-order assembly directly inhibits its cognate transcription activator PspF. Here we show that N-terminal amphipathic helices ahA and ahB in PspA HD1 are functional determinants involved in negative gene control and stress signal perception and its transduction via interactions with the PspBC membrane stress sensors and the inner membrane (IM). The amphipathic helices enable PspA to switch from a low-order gene regulator into an IM-bound high-order effector complex under membrane stress. Conserved residue proline 25 is involved in sequential use of the amphipathic helices and ahA IM interaction. Single molecule imaging of eGFP-PspA and its amphipathic helices variants in live Escherichia coli cells show distinct spatial and temporal organisations of PspA corresponding to its negative control and effector functions. These findings inform studies on the role of the Psp system in persister cell formation and cell envelope protection in bacterial pathogens and provide a basis for exploring the specialised roles of PspA homologues such as YjfJ, LiaH and Vipp1.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Molecular Biology",
title = "The N-Terminal Amphipathic Helices Determine Regulatory and Effector Functions of Phage Shock Protein A (PspA) in Escherichia coli",
pages = "1511-1498",
number = "7",
volume = "426",
doi = "10.1016/j.jmb.2013.12.016"
}

Jovanović, G., Mehta, P., McDonald, C., Davidson, A. C., Uzdavinys, P., Ying, L.,& Buck, M.. (2014). The N-Terminal Amphipathic Helices Determine Regulatory and Effector Functions of Phage Shock Protein A (PspA) in Escherichia coli. in Journal of Molecular Biology
Academic Press Ltd- Elsevier Science Ltd, London., 426(7), 1498-1511.
https://doi.org/10.1016/j.jmb.2013.12.016

Jovanović G, Mehta P, McDonald C, Davidson AC, Uzdavinys P, Ying L, Buck M. The N-Terminal Amphipathic Helices Determine Regulatory and Effector Functions of Phage Shock Protein A (PspA) in Escherichia coli. in Journal of Molecular Biology. 2014;426(7):1498-1511.
doi:10.1016/j.jmb.2013.12.016 .

Jovanović, Goran, Mehta, Parul, McDonald, Christopher, Davidson, Anthony C., Uzdavinys, Povilas, Ying, Liming, Buck, Martin, "The N-Terminal Amphipathic Helices Determine Regulatory and Effector Functions of Phage Shock Protein A (PspA) in Escherichia coli" in Journal of Molecular Biology, 426, no. 7 (2014):1498-1511,
https://doi.org/10.1016/j.jmb.2013.12.016 . .