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Science 22 November 1996:
Vol. 274. no. 5291, pp. 1385 - 1389
DOI: 10.1126/science.274.5291.1385
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Reports

Tricorn Protease--The Core of a Modular Proteolytic System

Tomohiro Tamura, Noriko Tamura, Zdenka Cejka, Reiner Hegerl, Friedrich Lottspeich, Wolfgang Baumeister *

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.

Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany.
*   To whom correspondence should be addressed.

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Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.
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