%0 Journal Article
%T Protein degradation by a component of the chaperonin-linked protease ClpP.
%A Ishikawa F
%A Homma M
%A Tanabe G
%A Uchihashi T
%J Genes Cells
%V 0
%N 0
%D 2024 Jul 4
%M 38965067
%F 2.3
%R 10.1111/gtc.13141
%X In cells, proteins are synthesized, function, and degraded (dead). Protein synthesis (spring) is important for the life of proteins. However, how proteins die is equally important for organisms. Proteases are secreted from cells and used as nutrients to break down external proteins. Proteases degrade unwanted and harmful cellular proteins. In eukaryotes, a large enzyme complex called the proteasome is primarily responsible for cellular protein degradation. Prokaryotes, such as bacteria, have similar protein degradation systems. In this review, we describe the structure and function of the ClpXP complex in the degradation system, which is an ATP-dependent protease in bacterial cells, with a particular focus on ClpP.