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Originally published In Press as doi:10.1074/jbc.M708440200 on January 10, 2008

J. Biol. Chem., Vol. 283, Issue 11, 6677-6686, March 14, 2008
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The F1F0-ATP Synthase Complex Influences the Assembly State of the Cytochrome bc1-Cytochrome Oxidase Supercomplex and Its Association with the TIM23 Machinery*

Sonika Saddar, Mary K. Dienhart, and Rosemary A. Stuart1

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 {Delta}su e and {Delta}su g null mutant strains exhibit decreased levels of COX enzyme activity but appear to have normal COX subunit protein levels. An altered stoichiometry of the cytochrome bc1-COX supercomplex was observed in mitochondria deficient in Su e and/or Su g, and a perturbation in the association of Cox4, a catalytically important subunit of the COX complex, was also detected. In addition, an increase in the level of the TIM23 translocase associated with the cytochrome bc1-COX supercomplex is observed in the absence of Su e and Su g. Together, our data highlight that a further level of complexity exists between the oxidative phosphorylation supercomplexes, whereby the organizational state of one complex, i.e. the ATP synthase, may influence that of another supercomplex, namely the cytochrome bc1-COX complex.


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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