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Adaptor protein controlled oligomerization activates the AAA+ protein ClpC
Author(s) -
Kirstein Janine,
Schlothauer Tilman,
Dougan David A,
Lilie Hauke,
Tischendorf Gilbert,
Mogk Axel,
Bukau Bernd,
Turgay Kürşad
Publication year - 2006
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601042
Subject(s) - biology , signal transducing adaptor protein , microbiology and biotechnology , signal transduction
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.