Chaperone-protease systems in regulation and protein quality control in Bacillus subtilis.
The Gram-positive model organism Bacillus subtilis is extremely well adapted to changing environmental conditions. The chaperone-protease ClpCP and other AAA+ proteases constitute an important component of the B. subtilis protein quality control system that is essential for survival during stress. In this review, we discuss recent discoveries concerning the molecular mechanism, regulation and localization of proteases and chaperones in B. subtilis.
Institut für Biologie-Mikrobiologie, Fachbereich Biologie, Chemie, Pharmazie, FU Berlin Königin-Luise-Str. 12-16, 14195 Berlin, Germany.
Noël
N
Molière
Kürşad
K
Turgay
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D049071:Endopeptidase Clp / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010447:Peptide Hydrolases; D049071:Endopeptidase Clp; D000251:Adenosine Triphosphatases