Membrane insertion of F0 c subunit of F0F1 ATPase depends on glycolipozyme MPIase and is stimulated by YidC

Biochem Biophys Res Commun. 2017 May 27;487(2):477-482. doi: 10.1016/j.bbrc.2017.04.095. Epub 2017 Apr 19.


The F0 c subunit of F0F1 ATPase (F0-c) possesses two membrane-spanning stretches with N- and C-termini exposed to the periplasmic (extracellular) side of the cytoplasmic membrane of E. coli. Although F0-c insertion has been extensively analyzed in vitro by means of protease protection assaying, it is unclear whether such assays allow elucidation of the insertion process faithfully, since the membrane-protected fragment, an index of membrane insertion, is a full-length polypeptide of F0-c, which is the same as the protease-resistant conformation without membrane insertion. We found that the protease-resistant conformation could be discriminated from membrane-insertion by including octyl glucoside on protease digestion. By means of this system, we found that F0-c insertion depends on MPIase, a glycolipozyme involved in membrane insertion, and is stimulated by YidC. In addition, we found that acidic phospholipids PG and CL transform F0-c into a protease-resistant form, while MPIase prevents the acquisition of such a protease-resistant conformation.

Keywords: C subunit; F(0)F(1) ATPase; Glycolipozyme; MPIase; Membrane protein insertion; YidC.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / chemistry
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / ultrastructure*
  • Lipid Bilayers / chemistry*
  • Membrane Transport Proteins / chemistry*
  • Membrane Transport Proteins / ultrastructure*
  • Mitochondrial Proton-Translocating ATPases / chemistry*
  • Mitochondrial Proton-Translocating ATPases / ultrastructure
  • Proton-Translocating ATPases / chemistry*
  • Proton-Translocating ATPases / ultrastructure*
  • Structure-Activity Relationship


  • Escherichia coli Proteins
  • Lipid Bilayers
  • Membrane Transport Proteins
  • YIDC protein, E coli
  • mitochondrial ATPase subunit c
  • Mitochondrial Proton-Translocating ATPases
  • Proton-Translocating ATPases