Home > Browse Issues > Vol.36 No.6
Progress in the Studies of ClpP: from Bacteria to Human Mitochondria
Chen Lin1,2#, Lan Linhua1,2#, He Haidong3#, Chen Zhibo3, She Shiqi3, Liu Yongzhang1,2, Lü Bin1,2*
1Institute of Biophysics, Wenzhou Medical University, Wenzhou 325035, China; 2School of Laboratory Medicine and Life Science, Wenzhou Medical University, Wenzhou 325035, China; 3The Second Clinical Medical School, Wenzhou Medical University, Wenzhou 325035, China
Abstract: Caseinolytic protease (ClpP) 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 hydrolysis 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 mitochondrial 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 of neurodegenerative diseases.
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