Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows

Proc Natl Acad Sci U S A. 2019 Mar 5;116(10):4250-4255. doi: 10.1073/pnas.1816556116. Epub 2019 Feb 13.


Mitochondrial ATP synthases form dimers, which assemble into long ribbons at the rims of the inner membrane cristae. We reconstituted detergent-purified mitochondrial ATP synthase dimers from the green algae Polytomella sp. and the yeast Yarrowia lipolytica into liposomes and examined them by electron cryotomography. Tomographic volumes revealed that ATP synthase dimers from both species self-assemble into rows and bend the lipid bilayer locally. The dimer rows and the induced degree of membrane curvature closely resemble those in the inner membrane cristae. Monomers of mitochondrial ATP synthase reconstituted into liposomes do not bend membrane visibly and do not form rows. No specific lipids or proteins other than ATP synthase dimers are required for row formation and membrane remodelling. Long rows of ATP synthase dimers are a conserved feature of mitochondrial inner membranes. They are required for cristae formation and a main factor in mitochondrial morphogenesis.

Keywords: ATP synthase; electron cryotomography; membrane curvature; mitochondria; subtomogram averaging.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chlorophyceae
  • Chlorophyta / metabolism
  • Lipid Bilayers / metabolism
  • Liposomes / ultrastructure
  • Mitochondria / metabolism
  • Mitochondrial Membranes / chemistry*
  • Mitochondrial Membranes / metabolism*
  • Mitochondrial Membranes / ultrastructure
  • Mitochondrial Proton-Translocating ATPases / chemistry*
  • Mitochondrial Proton-Translocating ATPases / metabolism*
  • Molecular Dynamics Simulation
  • Protein Conformation
  • Yarrowia / metabolism


  • Lipid Bilayers
  • Liposomes
  • Mitochondrial Proton-Translocating ATPases