Abstract
Controlled proteolysis underlies a vast diversity of protective and regulatory processes that are of key importance to cell fate. The unique molecular architecture of the widely conserved high temperature requirement A (HTRA) proteases has evolved to mediate critical aspects of ATP-independent protein quality control. The simple combination of a classic Ser protease domain and a carboxy-terminal peptide-binding domain produces cellular factors of remarkable structural and functional plasticity that allow cells to rapidly respond to the presence of misfolded or mislocalized polypeptides.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Enzyme Activation
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Humans
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Models, Biological
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Models, Molecular
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Molecular Chaperones / chemistry
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism
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PDZ Domains
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Photosynthesis
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Plant Proteins / chemistry
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Plant Proteins / genetics
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Plant Proteins / metabolism
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Serine Proteases / chemistry
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Serine Proteases / genetics
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Serine Proteases / metabolism*
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Temperature
Substances
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Bacterial Proteins
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Molecular Chaperones
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Plant Proteins
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Serine Proteases