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Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes

Item Type:Article
Title:Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes
Creators Name:Bornhoevd, C., Vogel, F., Neupert, W. and Reichert, A.S.
Abstract:The F1F0-ATP synthase in mitochondria, in addition to its function in energy transduction, has a structural role in determining cristae morphology. This depends on its ability to form dimeric and higher oligomeric supracomplexes. Here we show that mutants of the dimer-specific subunits e and g, which destabilize dimeric and oligomeric F1F0-ATP synthase supracomplexes, have a decreased mitochondrial membrane potential delta psi. The degree of destabilization correlated with the reduction of the membrane potential. The enzymatic activities of F1F0-ATP synthase and cytochrome c oxidase, maximal respiration rate, coupling of oxidative phosphorylation, and tubular mitochondrial morphology were not affected or only to a minor extent. In mutants lacking one or two coiled-coil domains of subunit e, the reduction of the mitochondrial membrane potential was not due to loss of mitochondrial DNA, a reduced capacity of oxidative phosphorylation, or to altered cristae morphology. We propose a role for the supracomplexes of the F1F0-ATP synthase in organizing microdomains within the inner membrane, ensuring optimal bioenergetic competence of mitochondria.
Keywords:Cytochromes, Dimerization, DNA, Membrane Potentials, Mitochondria, Mitochondrial Membranes, Mitochondrial Proton-Translocating ATPases, Oxygen, Phenotype, Phosphorylation, Protein Binding, Saccharomyces cerevisiae, Tertiary Protein Structure
Source:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology
Page Range:13990-13998
Date:19 May 2006
Official Publication:https://doi.org/10.1074/jbc.M512334200
PubMed:View item in PubMed

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