Abstract
Large macromolecular assemblies have evolved as a means of compartmentalizing reactions in organisms lacking membrane-bounded compartments. A tricorn-shaped protease was isolated from the archaeon Thermoplasma and was shown to form a multisubunit proteolytic complex. The 120-kilodalton monomer assembled to form a hexameric toroid that could assemble further into a capsid structure. Tricorn protease appeared to act as the core of a proteolytic system; when it interacted with several smaller proteins, it displayed multicatalytic activities.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Cloning, Molecular
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Cysteine Endopeptidases / metabolism
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Endopeptidases / chemistry*
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Endopeptidases / genetics
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Endopeptidases / isolation & purification
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Endopeptidases / metabolism*
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Genes, Bacterial
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Microscopy, Electron
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Models, Molecular
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Molecular Sequence Data
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Molecular Weight
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Multienzyme Complexes / metabolism
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Peptides / metabolism
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Proteasome Endopeptidase Complex
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Protein Conformation*
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Protein Folding
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Substrate Specificity
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Thermoplasma / enzymology*
Substances
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Multienzyme Complexes
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Peptides
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Recombinant Proteins
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Endopeptidases
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tricorn protease
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex