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J. Biol. Chem., Vol. 283, Issue 11, 6677-6686, March 14, 2008
The F1F0-ATP Synthase Complex Influences the Assembly State of the Cytochrome bc1-Cytochrome Oxidase Supercomplex and Its Association with the TIM23 Machinery*From the Department of Biological Sciences, Marquette University, Milwaukee, Wisconsin 53233
The enzyme complexes involved in mitochondrial oxidative phosphorylation are organized into higher ordered assemblies termed supercomplexes. Subunits e and g (Su e and Su g, respectively) are catalytically nonessential subunits of the F1F0-ATP synthase whose presence is required to directly support the stable dimerization of the ATP synthase complex. We report here that Su g and Su e are also important for securing the correct organizational state of the cytochrome bc1-cytochrome oxidase (COX) supercomplex. Mitochondria isolated from the
Received for publication, October 10, 2007 , and in revised form, December 18, 2007. * This work was supported by United States Public Health Service Grant RO1GM61573 (to R. A. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. 1 To whom correspondence should be addressed: Dept. of Biological Sciences, Marquette University, 530 N. 15th St., Milwaukee, WI 53233. Tel.: 414-288-1472; Fax: 414-288-7357; E-mail: rosemary.stuart{at}marquette.edu.
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