Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology
2010
Аутори
Joly, NicolasEngl, Christoph
Jovanović, Goran
Huvet, Maxime
Toni, Tina
Sheng, Xia
Stumpf, Michael P. H.
Buck, Martin
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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.
Кључне речи:
stress response / regulation of transcription / PspF / PspA / Psp proteins / phage shock protein responseИзвор:
FEMS Microbiology Reviews, 2010, 34, 5, 797-827Издавач:
- Oxford Univ Press, Oxford
Финансирање / пројекти:
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council
- Wellcome Trust VIP
- Biotechnology and Biological Sciences Research Council [BB/D521922/1, BB/F005210/1, BB/F005210/2] Funding Source: researchfish
- BBSRC [BB/F005210/2, BB/F005210/1] Funding Source: UKRI
DOI: 10.1111/j.1574-6976.2010.00240.x
ISSN: 0168-6445
PubMed: 20636484
WoS: 000280633500010
Scopus: 2-s2.0-77955127606
Институција/група
Institut za molekularnu genetiku i genetičko inženjerstvoTY - 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 . .