Tamura T, Tamura N, Cejka Z, Hegerl R, Lottspeich F, Baumeister W
Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany.
Science. 1996 Nov 22;274(5291):1385-9. 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.
大型大分子组装体已进化成为缺乏膜结合区室的生物体中分隔反应的一种方式。从嗜热栖热菌中分离出一种三触角状蛋白酶，它能形成多亚基蛋白水解复合物。120千道尔顿的单体组装形成六聚体环面，该环面还能进一步组装成衣壳结构。三触角蛋白酶似乎是蛋白水解系统的核心；当它与几种较小的蛋白质相互作用时，表现出多种催化活性。
