Details
| Original language | English |
|---|---|
| Pages (from-to) | 2061-2070 |
| Number of pages | 10 |
| Journal | EMBO Journal |
| Volume | 26 |
| Issue number | 8 |
| Publication status | Published - 22 Mar 2007 |
| Externally published | Yes |
Abstract
Cells of the soil bacterium Bacillus subtilis have to adapt to fast environmental changes in their natural habitat. Here, we characterized a novel system in which cells respond to heat shock by regulatory proteolysis of a transcriptional repressor CtsR. In B. subtilis, CtsR controls the synthesis of itself, the tyrosine kinase McsB, its activator McsA and the Hsp100/Clp proteins ClpC, ClpE and their cognate peptidase ClpP. The AAA+ protein family members ClpC and ClpE can form an ATP-dependent protease complex with ClpP and are part of the B. subtilis protein quality control system. The regulatory response is mediated by a proteolytic switch, which is formed by these proteins under heat-shock conditions, where the tyrosine kinase McsB acts as a regulated adaptor protein, which in its phosphorylated form activates the Hsp100/Clp protein ClpC and targets the repressor CtsR for degradation by the general protease ClpCP.
Keywords
- AAA+ proteins, Adaptor proteins, Heat shock regulation, Proteolysis, Tyrosine kinase
ASJC Scopus subject areas
- Neuroscience(all)
- General Neuroscience
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- General Biochemistry,Genetics and Molecular Biology
- Immunology and Microbiology(all)
- General Immunology and Microbiology
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In: EMBO Journal, Vol. 26, No. 8, 22.03.2007, p. 2061-2070.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The tyrosine kinase McsB is a regulated adaptor protein for ClpCP
AU - Kirstein, Janine
AU - Dougan, David A.
AU - Gerth, Ulf
AU - Hecker, Michael
AU - Turgay, Kürşad
N1 - Copyright: Copyright 2009 Elsevier B.V., All rights reserved.
PY - 2007/3/22
Y1 - 2007/3/22
N2 - Cells of the soil bacterium Bacillus subtilis have to adapt to fast environmental changes in their natural habitat. Here, we characterized a novel system in which cells respond to heat shock by regulatory proteolysis of a transcriptional repressor CtsR. In B. subtilis, CtsR controls the synthesis of itself, the tyrosine kinase McsB, its activator McsA and the Hsp100/Clp proteins ClpC, ClpE and their cognate peptidase ClpP. The AAA+ protein family members ClpC and ClpE can form an ATP-dependent protease complex with ClpP and are part of the B. subtilis protein quality control system. The regulatory response is mediated by a proteolytic switch, which is formed by these proteins under heat-shock conditions, where the tyrosine kinase McsB acts as a regulated adaptor protein, which in its phosphorylated form activates the Hsp100/Clp protein ClpC and targets the repressor CtsR for degradation by the general protease ClpCP.
AB - Cells of the soil bacterium Bacillus subtilis have to adapt to fast environmental changes in their natural habitat. Here, we characterized a novel system in which cells respond to heat shock by regulatory proteolysis of a transcriptional repressor CtsR. In B. subtilis, CtsR controls the synthesis of itself, the tyrosine kinase McsB, its activator McsA and the Hsp100/Clp proteins ClpC, ClpE and their cognate peptidase ClpP. The AAA+ protein family members ClpC and ClpE can form an ATP-dependent protease complex with ClpP and are part of the B. subtilis protein quality control system. The regulatory response is mediated by a proteolytic switch, which is formed by these proteins under heat-shock conditions, where the tyrosine kinase McsB acts as a regulated adaptor protein, which in its phosphorylated form activates the Hsp100/Clp protein ClpC and targets the repressor CtsR for degradation by the general protease ClpCP.
KW - AAA+ proteins
KW - Adaptor proteins
KW - Heat shock regulation
KW - Proteolysis
KW - Tyrosine kinase
UR - http://www.scopus.com/inward/record.url?scp=34247255841&partnerID=8YFLogxK
U2 - 10.1038/sj.emboj.7601655
DO - 10.1038/sj.emboj.7601655
M3 - Article
C2 - 17380125
AN - SCOPUS:34247255841
VL - 26
SP - 2061
EP - 2070
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 8
ER -