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Originally published In Press as doi:10.1074/jbc.C000427200 on July 28, 2000

J. Biol. Chem., Vol. 275, Issue 37, 28353-28355, September 15, 2000
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ACCELERATED PUBLICATION
Dimerization of Bovine F1-ATPase by Binding the Inhibitor Protein, IF1*

Elena CabezónDagger §, Ignacio ArechagaDagger , P. Jonathan, G. Butler, and John E. WalkerDagger ||

From Dagger  The Medical Research Council Dunn Human Nutrition Unit, Cambridge CB2 2XY and  The Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom

In mitochondria, the hydrolytic activity of ATP synthase is regulated by a natural inhibitor protein, IF1. The binding of IF1 to ATP synthase depends on pH values, and below neutrality, IF1 forms a stable complex with the enzyme. Bovine IF1 has two oligomeric states, dimer and tetramer, depending on pH values. At pH 6.5, where it is active, IF1 dimerizes by formation of an antiparallel alpha -helical coiled-coil in its C-terminal region. This arrangement places the inhibitory N-terminal regions in opposition, implying that active dimeric IF1 can bind two F1 domains simultaneously. Evidence of dimerization of F1-ATPase by binding to IF1 is provided by gel filtration chromatography, analytical ultracentrifugation, and electron microscopy. At present, it is not known whether IF1 can bring about the dimerization of the F1F0-ATPase complex.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported during part of this work by an European Molecular Biology Organization fellowship and by a Training and Mobility of Researchers Marie Curie research training grant from the European Community.

|| To whom correspondence should be addressed: The Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, U.K. Tel.: 0044-1223-252701; Fax: 0044-1223-252705; E-mail: walker@mrc-dunn.cam.ac.uk.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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