The tyrosine kinase McsB is a regulated adaptor protein for ClpCP

authored by: Janine Kirstein, David A. Dougan, Ulf Gerth, Michael Hecker, Kürşad Turgay
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.
External Organisation(s): Freie Universität Berlin (FU Berlin)
La Trobe University
University of Greifswald
Type: Article
Journal: EMBO Journal
Volume: 26
Pages: 2061-2070
No. of pages: 10
ISSN: 0261-4189
Publication date: 22.03.2007
Publication status: Published
Peer reviewed: Yes
ASJC Scopus subject areas: General Neuroscience, Molecular Biology, General Biochemistry,Genetics and Molecular Biology, General Immunology and Microbiology
Electronic version(s): https://doi.org/10.1038/sj.emboj.7601655 (Access: Closed)
http://europepmc.org/articles/pmc1852781?pdf=render (Access: Open)

BibTeX

@article{bd25d458752e41d08c0d5caf0761c635,
title = "The tyrosine kinase McsB is a regulated adaptor protein for ClpCP",
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",
author = "Janine Kirstein and Dougan, {David A.} and Ulf Gerth and Michael Hecker and K{\"u}r{\c s}ad Turgay",
note = "Copyright: Copyright 2009 Elsevier B.V., All rights reserved.",
year = "2007",
month = mar,
day = "22",
doi = "10.1038/sj.emboj.7601655",
language = "English",
volume = "26",
pages = "2061--2070",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "8",
}