Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. Joly, N., Engl, C., Jovanovic, G., Huvet, M., Toni, T., Sheng, X., Stumpf, M. P., & Buck, M. FEMS Microbiol Rev, 34(5):797–827, 2010. ![Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The bacterial phage shock protein (Psp) response functions to help cells manage the impacts of agents impairing cell membrane function. The system has relevance to biotechnology and to medicine. Originally discovered in Escherichia coli, Psp proteins and homologues are found in Gram-positive and Gram-negative bacteria, in archaea and in plants. Study of the E. coli and Yersinia enterocolitica Psp systems provides insights into how membrane-associated sensory Psp proteins might perceive membrane stress, signal to the transcription apparatus and use an ATP-hydrolysing transcription activator to produce effector proteins to overcome the stress. Progress in understanding the mechanism of signal transduction by the membrane-bound Psp proteins, regulation of the psp gene-specific transcription activator and the cell biology of the system is presented and discussed. Many features of the action of the Psp system appear to be dominated by states of self-association of the master effector, PspA, and the transcription activator, PspF, alongside a signalling pathway that displays strong conditionality in its requirement.
@article{joly_managing_2010,
title = {Managing membrane stress: the phage shock protein ({Psp}) response, from molecular mechanisms to physiology},
volume = {34},
issn = {1574-6976 (Electronic) 0168-6445 (Linking)},
url = {http://www.ncbi.nlm.nih.gov/pubmed/20636484 http://onlinelibrary.wiley.com/store/10.1111/j.1574-6976.2010.00240.x/asset/j.1574-6976.2010.00240.x.pdf?v=1&t=hvtybnbb&s=a6a4edef9631e20a0e4f21844f8e1bee280aab42},
doi = {10.1111/j.1574-6976.2010.00240.x},
abstract = {The bacterial phage shock protein (Psp) response functions to help cells manage the impacts of agents impairing cell membrane function. The system has relevance to biotechnology and to medicine. Originally discovered in Escherichia coli, Psp proteins and homologues are found in Gram-positive and Gram-negative bacteria, in archaea and in plants. Study of the E. coli and Yersinia enterocolitica Psp systems provides insights into how membrane-associated sensory Psp proteins might perceive membrane stress, signal to the transcription apparatus and use an ATP-hydrolysing transcription activator to produce effector proteins to overcome the stress. Progress in understanding the mechanism of signal transduction by the membrane-bound Psp proteins, regulation of the psp gene-specific transcription activator and the cell biology of the system is presented and discussed. Many features of the action of the Psp system appear to be dominated by states of self-association of the master effector, PspA, and the transcription activator, PspF, alongside a signalling pathway that displays strong conditionality in its requirement.},
language = {eng},
number = {5},
journal = {FEMS Microbiol Rev},
author = {Joly, Nicolas and Engl, Christoph and Jovanovic, Goran and Huvet, Maxime and Toni, Tina and Sheng, Xia and Stumpf, Michael P.H. and Buck, Martin},
year = {2010},
pmid = {20636484},
keywords = {*Bacterial Physiological Phenomena, *Stress, Bacterial Proteins/*metabolism, Cell Membrane/*metabolism, Escherichia coli Proteins/chemistry/metabolism, Escherichia coli/physiology, Heat-Shock Proteins/*metabolism, Membrane Proteins/*metabolism, Physiological, Psp proteins, PspA, PspF, Signal Transduction, Trans-Activators/chemistry/metabolism, phage shock protein response, regulation of transcription, stress response},
pages = {797--827},
}
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