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Molecular & Cellular Proteomics 7:995-1004, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Characterization of Domain Interfaces in Monomeric and Dimeric ATP Synthase^*

Ilka Wittig, Jean Velours, Rosemary Stuart^¶ and Hermann Schägger^,||

From the Zentrum der Biologischen Chemie, Molekulare Bioenergetik, Cluster of Excellence "Macromolecular Complexes", Johann Wolfgang Goethe-Universität Frankfurt, D-60590 Frankfurt, Germany, L'Institut de Biochimie et Génétique Cellulaires, Université Victor Segalen, CNRS, F-33077 Bordeaux, France, and ^¶ Department of Biological Sciences, Marquette University, Milwaukee, Wisconsin 53233

We disassembled monomeric and dimeric yeast ATP synthase under mild conditions to identify labile proteins and transiently stable subcomplexes that had not been observed before. Specific removal of subunits , β, oligomycin sensitivity conferring protein (OSCP), and h disrupted the ATP synthase at the -₃β₃ rotor-stator interface. Loss of two F₁-parts from dimeric ATP synthase led to the isolation of a dimeric subcomplex containing membrane and peripheral stalk proteins thus identifying the membrane/peripheral stalk sectors immediately as the dimerizing parts of ATP synthase. Almost all subunit a was found associated with a ring of 10 c-subunits in two-dimensional blue native/SDS gels. We therefore postulate that c₁₀a₁-complex is a stable structure in resting ATP synthase until the entry of protons induces a breaking of interactions and stepwise rotation of the c-ring relative to the a-subunit in the catalytic mechanism. Dimeric subunit a was identified in SDS gels in association with two c₁₀-rings suggesting that a c₁₀a₂c₁₀-complex may constitute an important part of the monomer-monomer interface in dimeric ATP synthase that seems to be further tightened by subunits b, i, e, g, and h. In contrast to the monomer-monomer interface, the interface between dimers in higher oligomeric structures remains largely unknown. However, we could show that the natural inhibitor protein Inh1 is not required for oligomerization.

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