Details
| Original language | English |
|---|---|
| Pages (from-to) | 2306-2311 |
| Number of pages | 6 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 100 |
| Issue number | 5 |
| Early online date | 7 Jan 2003 |
| Publication status | Published - 4 Mar 2003 |
| Externally published | Yes |
Abstract
ClpC of Bacillus subtilis is an ATP-dependent HSP100/Clp protein involved in general stress survival. A complex of ClpC with the protease ClpP and the adaptor protein MecA also controls competence development by regulated proteolysis of the transcription factor ComK. We investigated the in vitro chaperone activity of ClpC and found that the presence of MecA was crucial for the major chaperone activities of ClpC. In particular, MecA enabled ClpC to solubilize and refold aggregated proteins. Finally, in the presence of ClpP, MecA allowed the ClpC-dependent degradation of unfolded or heat-aggregated proteins. This study demonstrates that adaptor proteins like MecA through interaction with their cognate ClpC proteins can have a dual role in the protein quality-control network by rescuing, or together with ClpP, by degrading, aggregated proteins. MecA can thereby coordinate substrate targeting with ClpC activation, adding another layer to the regulation of HSP100/Cp protein activity.
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In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, No. 5, 04.03.2003, p. 2306-2311.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - MecA, an adaptor protein necessary for ClpC chaperone activity
AU - Schlothauer, Tilman
AU - Mogk, Axel
AU - Dougan, David A.
AU - Bukau, Bernd
AU - Turgay, Kürşad
N1 - Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2003/3/4
Y1 - 2003/3/4
N2 - ClpC of Bacillus subtilis is an ATP-dependent HSP100/Clp protein involved in general stress survival. A complex of ClpC with the protease ClpP and the adaptor protein MecA also controls competence development by regulated proteolysis of the transcription factor ComK. We investigated the in vitro chaperone activity of ClpC and found that the presence of MecA was crucial for the major chaperone activities of ClpC. In particular, MecA enabled ClpC to solubilize and refold aggregated proteins. Finally, in the presence of ClpP, MecA allowed the ClpC-dependent degradation of unfolded or heat-aggregated proteins. This study demonstrates that adaptor proteins like MecA through interaction with their cognate ClpC proteins can have a dual role in the protein quality-control network by rescuing, or together with ClpP, by degrading, aggregated proteins. MecA can thereby coordinate substrate targeting with ClpC activation, adding another layer to the regulation of HSP100/Cp protein activity.
AB - ClpC of Bacillus subtilis is an ATP-dependent HSP100/Clp protein involved in general stress survival. A complex of ClpC with the protease ClpP and the adaptor protein MecA also controls competence development by regulated proteolysis of the transcription factor ComK. We investigated the in vitro chaperone activity of ClpC and found that the presence of MecA was crucial for the major chaperone activities of ClpC. In particular, MecA enabled ClpC to solubilize and refold aggregated proteins. Finally, in the presence of ClpP, MecA allowed the ClpC-dependent degradation of unfolded or heat-aggregated proteins. This study demonstrates that adaptor proteins like MecA through interaction with their cognate ClpC proteins can have a dual role in the protein quality-control network by rescuing, or together with ClpP, by degrading, aggregated proteins. MecA can thereby coordinate substrate targeting with ClpC activation, adding another layer to the regulation of HSP100/Cp protein activity.
UR - http://www.scopus.com/inward/record.url?scp=0037418224&partnerID=8YFLogxK
U2 - 10.1073/pnas.0535717100
DO - 10.1073/pnas.0535717100
M3 - Article
C2 - 12598648
AN - SCOPUS:0037418224
VL - 100
SP - 2306
EP - 2311
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 5
ER -