Progress and prospect of single-molecular ClpX ATPase researching system-a mini-review.

单分子 ClpX ATP 酶研究体系的进展与展望.

• 影响指数: 3.913
• 发表时间: Mar 2021 30
• 来源期刊: Gene
• DOI: 10.1016/j.gene.2021.145420
• PMID: 33434627
• 文章类型: Journal Article
• 中科院分区: Q2
• 方向: 生物
• 作者列表: Kang ZH,Liu YT,Gou Y,Deng QR,Hu ZY,Li GR

关键词: ClpX; ClpXP; E. coli; Optical tweezers; Protease; Single molecule

Mesh: ATPases Associated with Diverse Cellular Activities / chemistry physiology; Biomedical Research; Endopeptidase Clp / chemistry physiology; Escherichia coli / enzymology; Escherichia coli Proteins / chemistry physiology; Metabolic Networks and Pathways; Mitochondria / physiology; Models, Molecular; Molecular Chaperones / chemistry physiology; Molecular Motor Proteins / chemistry physiology; Molecular Structure; Single Molecule Imaging; Structure-Activity Relationship

Abstract

ClpXP in Escherichia coli is a proteasome degrading protein substrates. It consists of one hexamer of ATPase (ClpX) and two heptamers of peptidase (ClpP). The ClpX binds ATP and translocates the substrate protein into the ClpP chamber by binding and hydrolysis of ATP. At single molecular level, ClpX harnesses cycles of power stroke (dwell and burst) to unfold the substrates, then releases the ADP and Pi. Based on the construction and function of ClpXP, especially the recent progress on how ClpX unfold protein substrates, in this mini-review, a currently proposed single ClpX molecular model system detected by optical tweezers, and its prospective for the elucidation of the mechanism of force generation of ClpX in its power stroke and the subunit interaction with each other, were discussed in detail.

摘要

大肠杆菌中的ClpXP是降解蛋白酶体的蛋白质底物。它由一个ATP酶六聚体(ClpX)和两个肽酶七聚体(ClpP)组成。ClpX结合ATP并通过ATP的结合和水解将底物蛋白转运到ClpP室中。在单分子水平上,ClpX线束的动力冲程循环(停留和爆裂)以展开基板,然后释放ADP和Pi。基于ClpXP的结构和功能,特别是ClpX如何展开蛋白质底物的最新进展，在这个小型审查中，目前提出的单ClpX分子模型系统由光镊子检测，及其对阐明ClpX在其动力冲程中的力产生机制和亚基相互作用的前景，进行了详细讨论。