Tricorn Protease—The Core of a Modular Proteolytic System

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Science  22 Nov 1996:
Vol. 274, Issue 5291, pp. 1385-1389
DOI: 10.1126/science.274.5291.1385


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.

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