Is there a relationship between the supramolecular organization of the mitochondrial ATP synthase and the formation of cristae?

Biochim Biophys Acta. 2002 Sep 10;1555(1-3):174-80. doi: 10.1016/s0005-2728(02)00274-8.


Blue native polyacrylamide gel electrophoresis (BN-PAGE) analyses of detergent mitochondrial extracts have provided evidence that the yeast ATP synthase could form dimers. Cross-linking experiments performed on a modified version of the i-subunit of this enzyme indicate the existence of such ATP synthase dimers in the yeast inner mitochondrial membrane. We also show that the first transmembrane segment of the eukaryotic b-subunit (bTM1), like the two supernumerary subunits e and g, is required for dimerization/oligomerization of ATP synthases. Unlike mitochondria of wild-type cells that display a well-developed cristae network, mitochondria of yeast cells devoid of subunits e, g, or bTM1 present morphological alterations with an abnormal proliferation of the inner mitochondrial membrane. From these observations, we postulate that an anomalous organization of the inner mitochondrial membrane occurs due to the absence of ATP synthase dimers/oligomers. We provide a model in which the mitochondrial ATP synthase is a key element in cristae morphogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Dimerization
  • Intracellular Membranes / chemistry
  • Intracellular Membranes / enzymology*
  • Intracellular Membranes / ultrastructure
  • Microscopy, Electron
  • Microscopy, Fluorescence
  • Mitochondria / chemistry
  • Mitochondria / enzymology*
  • Mitochondria / ultrastructure
  • Mitochondrial Proton-Translocating ATPases / chemistry*
  • Saccharomyces cerevisiae


  • Mitochondrial Proton-Translocating ATPases