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真细菌蛋白酶体

Eubacterial proteasomes.

作者信息

Lupas A, Zühl F, Tamura T, Wolf S, Nagy I, De Mot R, Baumeister W

机构信息

Max-Planck-Institut für Biochemie, Martinsried, Germany.

出版信息

Mol Biol Rep. 1997 Mar;24(1-2):125-31. doi: 10.1023/a:1006803512761.

Abstract

Proteasomes are large, multisubunit proteases with highly conserved structures. The 26S proteasome of eukaryotes is an ATP-dependent enzyme of about 2 MDa, which acts as the central protease of the ubiquitin-dependent pathway of protein degradation. The core of the 26S complex is formed by the 20S proteasome, an ATP-independent, barrel-shaped protease of about 700 kDa, which has also been detected in archaebacteria and, more recently, in eubacteria. Currently, the distribution of 20S proteasomes in eubacteria appears limited to the actinomycetes, while most other eubacteria contain a related complex of simpler structure.

摘要

蛋白酶体是具有高度保守结构的大型多亚基蛋白酶。真核生物的26S蛋白酶体是一种约2兆道尔顿的ATP依赖性酶,它是蛋白质降解的泛素依赖性途径的核心蛋白酶。26S复合物的核心由20S蛋白酶体形成,这是一种约700千道尔顿的ATP非依赖性桶状蛋白酶,在古细菌中也有发现,最近在真细菌中也有发现。目前,20S蛋白酶体在真细菌中的分布似乎仅限于放线菌,而大多数其他真细菌含有结构更简单的相关复合物。

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