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

Gene. 2021 Mar 30:774:145420. doi: 10.1016/j.gene.2021.145420. Epub 2021 Jan 9.

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.

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

Publication types

  • Review

MeSH terms

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

Substances

  • Escherichia coli Proteins
  • Molecular Chaperones
  • Molecular Motor Proteins
  • Endopeptidase Clp
  • ClpX protein, E coli
  • ATPases Associated with Diverse Cellular Activities