中文摘要：

Caseinolytic protease（ClpP）是一种包含丝氨酸蛋白酶催化三联体结构域的ATP依赖的蛋白水解酶，广泛存在于原核生物以及真核生物的线粒体和叶绿体中。它通常与AAA＋家族的分子伴4gClpX结合形成ClpXV蛋白酶复合物，AAA＋家族成员能利用水解ATP提供的能量将蛋白底物去折叠，随后将底物分子转移至ClpP蛋白酶的水解腔体进行降解。ClpP蛋白酶对细胞内蛋白质量控制及维持体内稳态起到至关重要的作用。该文综述了近年来有关ClpP蛋白酶在结构、功能以及与细菌毒力的关系和有关药物开发等方面的研究。

英文摘要：

Caseinolytic protease （CIpP） is an energy-dependent serine protease. It is highly conserved throughout bacteria to eukaryotic mitochondria and chloroplasts. ClpP is usually in association with AAA＋ family of molecular chaperone to form ClpXP complex. The members of this family use the energy of ATP nyarolysis to unfold protein substrates and translocate them through a central pore and into the degradation chamber of ClpP. They play a vital role in the protein quality control within mitoehondrial matrix and the maintenance protein homeostasis. Here, we reviewed recent studies on the structures and functions of ClpP, as well as the bacterial virulence. We also summarized the studies of ClpP as a drug target for novel antibiotics, the potential target as an anti-cancer and treatment ofneurodegenerative diseases.