Jakob Fuhrmann the Heat - Shock Regulator CtsR
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چکیده
, 1323 (2009); 324 Science et al. Jakob Fuhrmann the Heat-Shock Regulator CtsR McsB Is a Protein Arginine Kinase That Phosphorylates and Inhibits This copy is for your personal, non-commercial use only. clicking here. colleagues, clients, or customers by , you can order high-quality copies for your If you wish to distribute this article to others here. following the guidelines can be obtained by Permission to republish or repurpose articles or portions of articles ): December 5, 2013 www.sciencemag.org (this information is current as of The following resources related to this article are available online at http://www.sciencemag.org/content/324/5932/1323.full.html version of this article at: including high-resolution figures, can be found in the online Updated information and services, http://www.sciencemag.org/content/suppl/2009/06/03/324.5932.1323.DC1.html can be found at: Supporting Online Material http://www.sciencemag.org/content/324/5932/1323.full.html#related found at: can be related to this article A list of selected additional articles on the Science Web sites http://www.sciencemag.org/content/324/5932/1323.full.html#ref-list-1 , 4 of which can be accessed free: cites 19 articles This article 5 article(s) on the ISI Web of Science cited by This article has been http://www.sciencemag.org/content/324/5932/1323.full.html#related-urls 11 articles hosted by HighWire Press; see: cited by This article has been http://www.sciencemag.org/cgi/collection/molec_biol Molecular Biology subject collections: This article appears in the following
منابع مشابه
McsB is a protein arginine kinase that phosphorylates and inhibits the heat-shock regulator CtsR.
All living organisms face a variety of environmental stresses that cause the misfolding and aggregation of proteins. To eliminate damaged proteins, cells developed highly efficient stress response and protein quality control systems. We performed a biochemical and structural analysis of the bacterial CtsR/McsB stress response. The crystal structure of the CtsR repressor, in complex with DNA, pi...
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The heat-inducible CtsR regulon of Bacillus subtilis codes for three Clp proteins with chaperone or protease activity. While the importance of ClpC and ClpP has been elucidated for a wide range of cellular adaptation processes, this study deals with the physiological role of B. subtilis ClpE. Northern experiments and reporter gene analyses revealed that ClpE is essential both for efficient CtsR...
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In a recent study we demonstrated that a high-hydrostatic-pressure-tolerant isolate of Listeria monocytogenes lacks a codon in the class 3 heat shock regulator gene ctsR. This mutation in the region that encodes four consecutive glycines was directly responsible for the observed piezotolerance, increased stress resistance, and reduced virulence. The aim of the present study was to determine whe...
متن کاملA tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis.
The soil bacterium Bacillus subtilis possesses a fine-tuned and complex heat stress response system. The repressor CtsR, whose activity is regulated by its modulators McsA and McsB, controls the expression of the cellular protein quality control genes clpC, clpE and clpP. Here, we show that the interaction of McsA and McsB with CtsR results in the formation of a ternary complex that not only pr...
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Among Gram-positive bacteria, CtsR (Class Three Stress gene Repressor) mainly regulates the expression of genes encoding the Clp ATPases and the ClpP protease. To gain a better understanding of the biological significance of the CtsR regulon in response to heat-shock conditions, we performed a global proteomic analysis of Lactobacillus plantarum WCFS1 and ΔctsR mutant strains under optimal or h...
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