Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphatases / metabolism
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Bacillus subtilis / enzymology*
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Bacillus subtilis / genetics
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Bacillus subtilis / metabolism
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Bacterial Proteins / metabolism*
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Endopeptidase Clp / metabolism
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Gene Expression Regulation, Bacterial
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Heat-Shock Proteins / genetics
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Heat-Shock Proteins / metabolism
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Molecular Chaperones / metabolism*
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Peptide Hydrolases / metabolism*
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Substrate Specificity
Substances
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Bacterial Proteins
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Heat-Shock Proteins
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Molecular Chaperones
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Peptide Hydrolases
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Endopeptidase Clp
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Adenosine Triphosphatases