The ATP synthase is involved in generating mitochondrial cristae morphology.

TitleThe ATP synthase is involved in generating mitochondrial cristae morphology.
Publication TypeJournal Article
Year of Publication2002
AuthorsPaumard, P, Vaillier, J, Coulary, B, Schaeffer, J, Soubannier, V, Mueller, DM, Brèthes, D, di Rago, J-P, Velours, J
JournalEMBO J
Volume21
Issue3
Pagination221-30
Date Published2002 Feb 01
ISSN0261-4189
KeywordsDimerization, Intracellular Membranes, Microscopy, Electron, Mitochondria, Mitochondrial Proton-Translocating ATPases, Models, Molecular, Saccharomyces cerevisiae
Abstract

The inner membrane of the mitochondrion folds inwards, forming the cristae. This folding allows a greater amount of membrane to be packed into the mitochondrion. The data in this study demonstrate that subunits e and g of the mitochondrial ATP synthase are involved in generating mitochondrial cristae morphology. These two subunits are non-essential components of ATP synthase and are required for the dimerization and oligomerization of ATP synthase. Mitochondria of yeast cells deficient in either subunits e or g were found to have numerous digitations and onion-like structures that correspond to an uncontrolled biogenesis and/or folding of the inner mitochondrial membrane. The present data show that there is a link between dimerization of the mitochondrial ATP synthase and cristae morphology. A model is proposed of the assembly of ATP synthase dimers, taking into account the oligomerization of the yeast enzyme and earlier data on the ultrastructure of mitochondrial cristae, which suggests that the association of ATP synthase dimers is involved in the control of the biogenesis of the inner mitochondrial membrane.

DOI10.1093/emboj/21.3.221
Alternate JournalEMBO J.
Citation Key10.1093/emboj/21.3.221
PubMed ID11823415
PubMed Central IDPMC125827
Grant ListGM44412 / GM / NIGMS NIH HHS / United States