Details
| Original language | English |
|---|---|
| Pages (from-to) | 1481-1491 |
| Number of pages | 11 |
| Journal | EMBO Journal |
| Volume | 25 |
| Issue number | 7 |
| Publication status | Published - 9 Mar 2006 |
| Externally published | Yes |
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
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. 25, No. 7, 09.03.2006, p. 1481-1491.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Adaptor protein controlled oligomerization activates the AAA + protein ClpC
AU - Kirstein, Janine
AU - Schlothauer, Tilman
AU - Dougan, David A.
AU - Lilie, Hauke
AU - Tischendorf, Gilbert
AU - Mogk, Axel
AU - Bukau, Bernd
AU - Turgay, Kürşad
N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2006/3/9
Y1 - 2006/3/9
N2 - 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.
AB - 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.
KW - AAA +
KW - Adaptorprotein
KW - Chaperones
KW - HSP100/Clp
KW - Proteolysis
UR - http://www.scopus.com/inward/record.url?scp=33645741669&partnerID=8YFLogxK
U2 - 10.1038/sj.emboj.7601042
DO - 10.1038/sj.emboj.7601042
M3 - Article
C2 - 16525504
AN - SCOPUS:33645741669
VL - 25
SP - 1481
EP - 1491
JO - EMBO Journal
JF - EMBO Journal
SN - 0261-4189
IS - 7
ER -