Adaptor protein controlled oligomerization activates the AAA + protein ClpC

verfasst von: Janine Kirstein, Tilman Schlothauer, David A. Dougan, Hauke Lilie, Gilbert Tischendorf, Axel Mogk, Bernd Bukau, Kürşad Turgay
Abstract: The AAA + protein ClpC is not only involved in the removal of misfolded and aggregated proteins but also controls, through regulated proteolysis, key steps of several developmental processes in the Gram-positive bacterium Bacillus subtilis. In contrast to other AAA + proteins, ClpC is unable to mediate these processes without an adaptor protein like MecA. Here, we demonstrate that the general activation of ClpC is based upon the ability of MecA to participate in the assembly of an active and substrate-recognizing higher oligomer consisting of ClpC and the adaptor protein, which is a prerequisite for all activities of this AAA + protein. Using hybrid proteins of ClpA and ClpC, we identified the N-terminal and the Linker domain of the first AAA + domain of ClpC as the essential MecA interaction sites. This new adaptor-mediated mechanism adds another layer of control to the regulation of the biological activity of AAA + proteins.
Externe Organisation(en): Freie Universität Berlin (FU Berlin)
Ruprecht-Karls-Universität Heidelberg
La Trobe University
Martin-Luther-Universität Halle-Wittenberg
Typ: Artikel
Journal: EMBO Journal
Band: 25
Seiten: 1481-1491
Anzahl der Seiten: 11
ISSN: 0261-4189
Publikationsdatum: 09.03.2006
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Allgemeine Neurowissenschaft, Molekularbiologie, Allgemeine Biochemie, Genetik und Molekularbiologie, Allgemeine Immunologie und Mikrobiologie
Elektronische Version(en): https://doi.org/10.1038/sj.emboj.7601042 (Zugang: Geschlossen)
http://europepmc.org/articles/pmc1440321?pdf=render (Zugang: Offen)

BibTeX

@article{907bf2c74dfa40a1aa0f4091c0483b2d,
title = "Adaptor protein controlled oligomerization activates the AAA + protein ClpC",
abstract = "The AAA + protein ClpC is not only involved in the removal of misfolded and aggregated proteins but also controls, through regulated proteolysis, key steps of several developmental processes in the Gram-positive bacterium Bacillus subtilis. In contrast to other AAA + proteins, ClpC is unable to mediate these processes without an adaptor protein like MecA. Here, we demonstrate that the general activation of ClpC is based upon the ability of MecA to participate in the assembly of an active and substrate-recognizing higher oligomer consisting of ClpC and the adaptor protein, which is a prerequisite for all activities of this AAA + protein. Using hybrid proteins of ClpA and ClpC, we identified the N-terminal and the Linker domain of the first AAA + domain of ClpC as the essential MecA interaction sites. This new adaptor-mediated mechanism adds another layer of control to the regulation of the biological activity of AAA + proteins.",
keywords = "AAA +, Adaptorprotein, Chaperones, HSP100/Clp, Proteolysis",
author = "Janine Kirstein and Tilman Schlothauer and Dougan, {David A.} and Hauke Lilie and Gilbert Tischendorf and Axel Mogk and Bernd Bukau and K{\"u}r{\c s}ad Turgay",
note = "Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",
year = "2006",
month = mar,
day = "9",
doi = "10.1038/sj.emboj.7601042",
language = "English",
volume = "25",
pages = "1481--1491",
journal = "EMBO Journal",
issn = "0261-4189",
publisher = "Springer Science and Business Media Deutschland GmbH",
number = "7",
}