Progress and Prospect of Single-molecular ClpX ATPase Researching system-a mini-review.

Progress and Prospect of Single-molecular ClpX ATPase Researching system-a mini-review. Gene. 2021 Jan 09;:145420 Authors: Kang ZH, Liu YT, Gou Y, Deng QR, Hu ZY, Li GR 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. PMID: 33434627 [PubMed - as supplied by publisher]
Source: Gene - Category: Genetics & Stem Cells Authors: Tags: Gene Source Type: research