Protein Degradation by a Component of the Chaperonin-linked Protease ClpP

Overview

Journal Genes Cells

Specialties Cell Biology
Molecular Biology

Date 2024 Jul 4

PMID 38965067

Authors

Fumihiro Ishikawa

Michio Homma

Genzoh Tanabe

Takayuki Uchihashi

Affiliations

Soon will be listed here.

Abstract

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.

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Protein degradation by a component of the chaperonin-linked protease ClpP.

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PMID: 38965067 PMC: 11448347. DOI: 10.1111/gtc.13141.

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