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Eukaryotic Cell, February 2005, p. 346-355, Vol. 4, No. 2
1535-9778/05/$08.00+0     doi:10.1128/EC.4.2.346-355.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Functional Analysis of Subunit e of the F1Fo-ATP Synthase of the Yeast Saccharomyces cerevisiae: Importance of the N-Terminal Membrane Anchor Region

Valerie Everard-Gigot,1 Cory D. Dunn,2 Brigid M. Dolan,1 Susanne Brunner,1 Robert E. Jensen,2 and Rosemary A. Stuart1*

Department of Biological Sciences, Marquette University, Milwaukee, Wisconsin,1 Johns Hopkins University School of Medicine, Baltimore, Maryland2

Received 15 October 2004/ Accepted 13 December 2004

Mitochondrial F1Fo-ATP synthase complexes do not exist as physically independent entities but rather form dimeric and possibly oligomeric complexes in the inner mitochondrial membrane. Stable dimerization of two F1Fo-monomeric complexes involves the physical association of two membrane-embedded Fo-sectors. Previously, formation of the ATP synthase dimeric-oligomeric network was demonstrated to play a critical role in modulating the morphology of the mitochondrial inner membrane. In Saccharomyces cerevisiae, subunit e (Su e) of the Fo-sector plays a central role in supporting ATP synthase dimerization. The Su e protein is anchored to the inner membrane via a hydrophobic region located at its N-terminal end. The hydrophilic C-terminal region of Su e resides in the intermembrane space and contains a conserved coiled-coil motif. In the present study, we focused on characterizing the importance of these regions for the function of Su e. We created a number of C-terminal-truncated derivatives of the Su e protein and expressed them in the Su e null yeast mutant. Mitochondria were isolated from the resulting transformant strains, and a number of functions of Su e were analyzed. Our results indicate that the N-terminal hydrophobic region plays important roles in the Su e-dependent processes of mitochondrial DNA maintenance, modulation of mitochondrial morphology, and stabilization of the dimer-specific Fo subunits, subunits g and k. Furthermore, we show that the C-terminal coiled-coil region of Su e functions to stabilize the dimeric form of detergent-solubilized ATP synthase complexes. Finally, we propose a model to explain how Su e supports the assembly of the ATP synthase dimers-oligomers in the mitochondrial membrane.

* Corresponding author. Mailing address: Department of Biological Sciences, Marquette University, 530 N. 15th St., Milwaukee, WI 53233. Phone: (414) 288-1472. Fax: (414) 288-7357. E-mail: rosemary.stuart{at}marquette.edu.

Eukaryotic Cell, February 2005, p. 346-355, Vol. 4, No. 2
1535-9778/05/$08.00+0     doi:10.1128/EC.4.2.346-355.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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