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MecA, an adaptor protein necessary for ClpC chaperone activity
- Source :
- Proceedings of the National Academy of Sciences of the United States. March 4, 2003, Vol. 100 Issue 5, p2306, 6 p.
- Publication Year :
- 2003
-
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/Clp protein activity.
- Subjects :
- Bacillus subtilis -- Genetic aspects
Bacillus subtilis -- Physiological aspects
Adenosine triphosphate -- Physiological aspects
Bacterial proteins -- Physiological aspects
Bacterial proteins -- Genetic aspects
Genetic transcription -- Physiological aspects
Proteases -- Physiological aspects
Proteases -- Genetic aspects
Genetic regulation -- Analysis
Protein folding -- Genetic aspects
Protein folding -- Physiological aspects
Science and technology
Subjects
Details
- ISSN :
- 00278424
- Volume :
- 100
- Issue :
- 5
- Database :
- Gale General OneFile
- Journal :
- Proceedings of the National Academy of Sciences of the United States
- Publication Type :
- Academic Journal
- Accession number :
- edsgcl.99148279