title: Supramolecular organization of the yeast F1Fo-ATP synthase.
abstract: BACKGROUND
  The yeast mitochondrial F(1)F(o)-ATP synthase is a large complex of 600 kDa that uses the proton electrochemical gradient generated by the respiratory chain to catalyse ATP synthesis from ADP and P(i). For a large range of organisms, it has been shown that mitochondrial ATP synthase adopts oligomeric structures. Moreover, several studies have suggested that a link exists between ATP synthase and mitochondrial morphology.
  
  
  CONCLUSIONS
  In order to understand the link between ATP synthase oligomerization and mitochondrial morphology, more information is needed on the supramolecular organization of this enzyme within the inner mitochondrial membrane. We have conducted an electron microscopy study on wild-type yeast mitochondria at different levels of organization from spheroplast to isolated ATP synthase complex. Using electron tomography, freeze-fracture, negative staining and image processing, we show that cristae form a network of lamellae, on which ATP synthase dimers assemble in linear and regular arrays of oligomers.
  
  
  CONCLUSIONS
  Our results shed new light on the supramolecular organization of the F(1)F(o)-ATP synthase and its potential role in mitochondrial morphology.
authors.affiliation: CNRS, Interactions Cellulaires et Moléculaires, UMR 6026, Université Rennes 1, Campus de Beaulieu, Bâtiment 13, F-35042 Rennes cedex, France.
authors.forename: Daniel
authors.initials: D
authors.lastname: Thomas
authors.forename: Patrick
authors.initials: P
authors.lastname: Bron
authors.forename: Théodore
authors.initials: T
authors.lastname: Weimann
authors.forename: Alain
authors.initials: A
authors.lastname: Dautant
authors.forename: Marie-France
authors.initials: MF
authors.lastname: Giraud
authors.forename: Patrick
authors.initials: P
authors.lastname: Paumard
authors.forename: Bénédicte
authors.initials: B
authors.lastname: Salin
authors.forename: Annie
authors.initials: A
authors.lastname: Cavalier
authors.forename: Jean
authors.initials: J
authors.lastname: Velours
authors.forename: Daniel
authors.initials: D
authors.lastname: Brèthes
mesh_terms: D020285:Cryoelectron Microscopy; D019281:Dimerization; D008928:Mitochondria / Q000201:enzymology*; D051336:Mitochondrial Membranes / Q000201:enzymology / Q000648:ultrastructure; D024101:Mitochondrial Proteins / Q000737:chemistry* / Q000378:metabolism; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D020836:Protein Structure, Quaternary; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D013104:Spheroplasts / Q000201:enzymology / Q000648:ultrastructure
chemical_list: D024101:Mitochondrial Proteins; D020033:Protein Isoforms; D029701:Saccharomyces cerevisiae Proteins; C474451:F1F0-ATP synthase; D025261:Mitochondrial Proton-Translocating ATPases