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伴侣蛋白酶连接的蛋白酶 ClpP 成分介导的蛋白质降解。

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

机构信息

Faculty of Pharmacy, Kindai University, Osaka, Japan.

Department of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya, Japan.

出版信息

Genes Cells. 2024 Sep;29(9):695-709. doi: 10.1111/gtc.13141. Epub 2024 Jul 4.

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.

摘要

在细胞中,蛋白质被合成、发挥功能和降解(死亡)。蛋白质的合成(春天)对蛋白质的生命至关重要。然而,蛋白质的死亡对于生物体同样重要。蛋白酶从细胞中分泌出来,并被用作营养物质来分解外部蛋白质。蛋白酶降解不需要的和有害的细胞蛋白质。在真核生物中,一种叫做蛋白酶体的大型酶复合物主要负责细胞内蛋白质的降解。原核生物,如细菌,也有类似的蛋白质降解系统。在这篇综述中,我们描述了 ClpXP 复合物在细菌细胞中作为一种 ATP 依赖的蛋白酶的降解系统中的结构和功能,特别关注 ClpP。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1c0/11448347/c9c6b760a8cb/GTC-29-695-g003.jpg

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