Protein degradation by a component of the chaperonin‐linked protease <scp>ClpP</scp>

DOI Web Site 被引用文献1件 参考文献92件 オープンアクセス
  • Fumihiro Ishikawa
    Faculty of Pharmacy Kindai University Osaka Japan
  • Michio Homma
    Department of Biomolecular Engineering, Graduate School of Engineering Nagoya University Nagoya Japan
  • Genzoh Tanabe
    Faculty of Pharmacy Kindai University Osaka Japan
  • Takayuki Uchihashi
    Division of Material Science, Graduate School of Science Nagoya University Nagoya Japan

書誌事項

公開日
2024-07-04
資源種別
journal article
権利情報
  • http://creativecommons.org/licenses/by/4.0/
DOI
  • 10.1111/gtc.13141
公開者
Wiley

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説明

<jats:title>Abstract</jats:title><jats:p>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.</jats:p>

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