The N-Terminal Amphipathic Helices Determine Regulatory and Effector Functions of Phage Shock Protein A (PspA) in Escherichia coli
Samo za registrovane korisnike
2014
Autori
Jovanović, GoranMehta, Parul
McDonald, Christopher
Davidson, Anthony C.
Uzdavinys, Povilas
Ying, Liming
Buck, Martin
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Ključne reči:
PspA HD1 / proline 25 / negative regulation of AAA / membrane stress / high-order oligomersIzvor:
Journal of Molecular Biology, 2014, 426, 7, 1498-1511Izdavač:
- Academic Press Ltd- Elsevier Science Ltd, London
Finansiranje / projekti:
- Biotechnology and Biological Sciences Research Council [BB/G00594X/1]
- Leverhulme Trust [RPG-2012-705]
- BBSRC [BB/G00594X/1] Funding Source: UKRI
DOI: 10.1016/j.jmb.2013.12.016
ISSN: 0022-2836
PubMed: 24361331
WoS: 000334478000013
Scopus: 2-s2.0-84895929192
Institucija/grupa
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 . .