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          Institute: MPI für Biophysik     Collection: Abt. Strukturbiologie     Display Documents



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ID: 571443.0, MPI für Biophysik / Abt. Strukturbiologie
Macromolecular organization of ATP synthase and complex I in whole mitochondria
Authors:Davies, Karen M.; Strauss, Mike; Daum, Bertram; Kief, Jan H.; Osiewacz, Heinz D.; Rycovska, Adriana; Zickermann, Volker; Kühlbrandt, Werner
Language:English
Date of Publication (YYYY-MM-DD):2011
Title of Journal:Proceedings of the National Academy of Sciences of the United States of America
Journal Abbrev.:Proc. Natl. Acad. Sci. USA
Volume:108
Issue / Number:34
Start Page:14121
End Page:14126
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:We used electron cryotomography to study the molecular arrangement of large respiratory chain complexes in mitochondria from bovine heart, potato, and three types of fungi. Long rows of ATP synthase dimers were observed in intact mitochondria and cristae membrane fragments of all species that were examined. The dimer rows were found exclusively on tightly curved cristae edges. The distance between dimers along the rows varied, but within the dimer the distance between F1 heads was constant. The angle between monomers in the dimer was 70° or above. Complex I appeared as L-shaped densities in tomograms of reconstituted proteoliposomes. Similar densities were observed in flat membrane regions of mitochondrial membranes from all species except Saccharomyces cerevisiae and identified as complex I by quantum-dot labeling. The arrangement of respiratory chain proton pumps on flat cristae membranes and ATP synthase dimer rows along cristae edges was conserved in all species investigated. We propose that the supramolecular organization of respiratory chain complexes as proton sources and ATP synthase rows as proton sinks in the mitochondrial cristae ensures optimal conditions for efficient ATP synthesis.
Free Keywords:cryoelectron tomography; subtomogram averaging; membrane curvature; membrane potential; mitochondrial ultrastructure
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Strukturbiologie
MPI für Biophysik/Abteilung Molekulare Membranbiologie
External Affiliations:Mitochondrial Biology, Medical School, Goethe University Frankfurt am Main, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany;
Mitochondrial Biology, Frankfurt Institute for Molecular Life Sciences, Max-von-Laue-Strasse 9, 60438 Frankfurt am Main, Germany;
Molecular Developmental Biology, Goethe University, Max-von-Laue-Strasse 9, Germany;
Deutsche Forschungsgemeinschaft Cluster of Excellence Frankfurt “Macromolecular Complexes”, 60438 Frankfurt, Germany;
Medical Faculty, Molecular Bioenergetics, Goethe University, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany
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