TY  - JOUR
AU  - Joly, Nicolas
AU  - Engl, Christoph
AU  - Jovanović, Goran
AU  - Huvet, Maxime
AU  - Toni, Tina
AU  - Sheng, Xia
AU  - Stumpf, Michael P. H.
AU  - Buck, Martin
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/454
AB  - 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.
PB  - Oxford Univ Press, Oxford
T2  - FEMS Microbiology Reviews
T1  - Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology
EP  - 827
IS  - 5
SP  - 797
VL  - 34
DO  - 10.1111/j.1574-6976.2010.00240.x
ER  - 

@article{
author = "Joly, Nicolas and Engl, Christoph and Jovanović, Goran and Huvet, Maxime and Toni, Tina and Sheng, Xia and Stumpf, Michael P. H. and Buck, Martin",
year = "2010",
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.",
publisher = "Oxford Univ Press, Oxford",
journal = "FEMS Microbiology Reviews",
title = "Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology",
pages = "827-797",
number = "5",
volume = "34",
doi = "10.1111/j.1574-6976.2010.00240.x"
}

Joly, N., Engl, C., Jovanović, G., Huvet, M., Toni, T., Sheng, X., Stumpf, M. P. H.,& Buck, M.. (2010). Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. in FEMS Microbiology Reviews
Oxford Univ Press, Oxford., 34(5), 797-827.
https://doi.org/10.1111/j.1574-6976.2010.00240.x

Joly N, Engl C, Jovanović G, Huvet M, Toni T, Sheng X, Stumpf MPH, Buck M. Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. in FEMS Microbiology Reviews. 2010;34(5):797-827.
doi:10.1111/j.1574-6976.2010.00240.x .

Joly, Nicolas, Engl, Christoph, Jovanović, Goran, Huvet, Maxime, Toni, Tina, Sheng, Xia, Stumpf, Michael P. H., Buck, Martin, "Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology" in FEMS Microbiology Reviews, 34, no. 5 (2010):797-827,
https://doi.org/10.1111/j.1574-6976.2010.00240.x . .