蛋白酶Ti（Clp），一种大肠杆菌中的多组分ATP依赖性蛋白酶。

Protease Ti (Clp), a multi-component ATP-dependent protease in Escherichia coli.

作者信息

Chung C H, Seol J H, Kang M S

机构信息

Department of Molecular Biology and SRC for Cell Differentiation, College of Natural Sciences, Seoul National University, Korea.

出版信息

Biol Chem. 1996 Sep;377(9):549-54.

PMID:9067252

Abstract

The ATP-dependent protease Ti(Clp) consists of two different multimeric components: ClpA containing ATP-cleaving sites and ClpP, with serine active sites for proteolysis. Here we summarize the most recent results on the structure and function of protease Ti. (1) The clpA gene has dual translational initiation sites and therefore encodes two polypeptides with sizes of 84 and 65 kDa. The abbreviated form of ClpA may play an important role in regulation of the ATP-dependent proteolysis, since it inhibits the ability of the 84-kDa ClpA in supporting the ClpP-mediated protein breakdown and the autodegradation of the 84-kDa ClpA. (2) ClpA contains two highly conserved sequences for ATP-binding: the first site is essential for oligomerization and the second site is responsible for ATP hydrolysis. (3) ATP hydrolysis by ClpA is required not only for assembly of the ClpA/ClpP complex but also for its rapid dissociation.

摘要

ATP 依赖性蛋白酶 Ti(Clp) 由两种不同的多聚体成分组成：含有 ATP 裂解位点的 ClpA 和具有蛋白水解丝氨酸活性位点的 ClpP。在此，我们总结了关于蛋白酶 Ti 结构与功能的最新研究成果。(1) clpA 基因有两个翻译起始位点，因此编码大小分别为 84 kDa 和 65 kDa 的两种多肽。ClpA 的缩写形式可能在 ATP 依赖性蛋白水解的调控中发挥重要作用，因为它抑制 84 kDa 的 ClpA 支持 ClpP 介导的蛋白质降解以及 84 kDa 的 ClpA 自身降解的能力。(2) ClpA 含有两个高度保守的 ATP 结合序列：第一个位点对于寡聚化至关重要，第二个位点负责 ATP 水解。(3) ClpA 水解 ATP 不仅是 ClpA/ClpP 复合体组装所必需的，也是其快速解离所必需的。