Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 2061-2070 |
| Seitenumfang | 10 |
| Fachzeitschrift | EMBO Journal |
| Jahrgang | 26 |
| Ausgabenummer | 8 |
| Publikationsstatus | Veröffentlicht - 22 März 2007 |
| Extern publiziert | Ja |
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.
ASJC Scopus Sachgebiete
- Neurowissenschaften (insg.)
- Allgemeine Neurowissenschaft
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Allgemeine Biochemie, Genetik und Molekularbiologie
- Immunologie und Mikrobiologie (insg.)
- Allgemeine Immunologie und Mikrobiologie
Zitieren
- Standard
- Harvard
- Apa
- Vancouver
- BibTex
- RIS
in: EMBO Journal, Jahrgang 26, Nr. 8, 22.03.2007, S. 2061-2070.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › 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 -