Details
| Original language | English |
|---|---|
| Pages (from-to) | 3435-3445 |
| Number of pages | 11 |
| Journal | EMBO Journal |
| Volume | 24 |
| Issue number | 19 |
| Publication status | Published - 5 Oct 2005 |
| Externally published | Yes |
Abstract
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 prevents the binding of CtsR to its target DNA, but also results in a subsequent phosphorylation of McsB, McsA and CtsR. We further demonstrate that McsB is a tyrosine kinase that needs McsA to become activated. ClpC inhibits the kinase activity of McsB, indicating a direct role in initiating CtsR-controlled heat shock response. Interestingly, the kinase domain of McsB is homologous to guanidino phosphotransferase domains originating from eukaryotic arginine and creatine kinases. Mutational analysis of key residues of the guanidino kinase domain demonstrated that McsB utilizes this domain to catalyze the tyrosine phosphorylation. McsB represents therefore a new kind of tyrosine kinase, driven by a guanidino phosphotransferase domain.
Keywords
- Bacillus, Heat shock response, Signal transduction, Tyrosine kinase
ASJC Scopus subject areas
- Neuroscience(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Immunology and Microbiology(all)
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In: EMBO Journal, Vol. 24, No. 19, 05.10.2005, p. 3435-3445.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A tyrosine kinase and its activator control the activity of the CtsR heat shock repressor in B. subtilis
AU - Kirstein, Janine
AU - Zühlke, Daniela
AU - Gerth, Ulf
AU - Turgay, Kürşad
AU - Hecker, Michael
N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/10/5
Y1 - 2005/10/5
N2 - 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 prevents the binding of CtsR to its target DNA, but also results in a subsequent phosphorylation of McsB, McsA and CtsR. We further demonstrate that McsB is a tyrosine kinase that needs McsA to become activated. ClpC inhibits the kinase activity of McsB, indicating a direct role in initiating CtsR-controlled heat shock response. Interestingly, the kinase domain of McsB is homologous to guanidino phosphotransferase domains originating from eukaryotic arginine and creatine kinases. Mutational analysis of key residues of the guanidino kinase domain demonstrated that McsB utilizes this domain to catalyze the tyrosine phosphorylation. McsB represents therefore a new kind of tyrosine kinase, driven by a guanidino phosphotransferase domain.
AB - 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 prevents the binding of CtsR to its target DNA, but also results in a subsequent phosphorylation of McsB, McsA and CtsR. We further demonstrate that McsB is a tyrosine kinase that needs McsA to become activated. ClpC inhibits the kinase activity of McsB, indicating a direct role in initiating CtsR-controlled heat shock response. Interestingly, the kinase domain of McsB is homologous to guanidino phosphotransferase domains originating from eukaryotic arginine and creatine kinases. Mutational analysis of key residues of the guanidino kinase domain demonstrated that McsB utilizes this domain to catalyze the tyrosine phosphorylation. McsB represents therefore a new kind of tyrosine kinase, driven by a guanidino phosphotransferase domain.
KW - Bacillus
KW - Heat shock response
KW - Signal transduction
KW - Tyrosine kinase
UR - http://www.scopus.com/inward/record.url?scp=27144440950&partnerID=8YFLogxK
U2 - 10.1038/sj.emboj.7600780
DO - 10.1038/sj.emboj.7600780
M3 - Article
C2 - 16163393
AN - SCOPUS:27144440950
VL - 24
SP - 3435
EP - 3445
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 19
ER -