A mitochondrial megachannel resides in monomeric F1FO ATP synthase

Nelli Mnatsakanyan (), Marc C. Llaguno, Youshan Yang, Yangyang Yan, Joachim Weber, Fred J. Sigworth and Elizabeth A. Jonas ()
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Nelli Mnatsakanyan: Yale University
Marc C. Llaguno: Yale University
Youshan Yang: Yale University
Yangyang Yan: Yale University
Joachim Weber: Texas Tech University
Fred J. Sigworth: Yale University
Elizabeth A. Jonas: Yale University

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract Purified mitochondrial ATP synthase has been shown to form Ca2+-activated, large conductance channel activity similar to that of mitochondrial megachannel (MMC) or mitochondrial permeability transition pore (mPTP) but the oligomeric state required for channel formation is being debated. We reconstitute purified monomeric ATP synthase from porcine heart mitochondria into small unilamellar vesicles (SUVs) with the lipid composition of mitochondrial inner membrane and analyze its oligomeric state by electron cryomicroscopy. The cryo-EM density map reveals the presence of a single ATP synthase monomer with no density seen for a second molecule tilted at an 86o angle relative to the first. We show that this preparation of SUV-reconstituted ATP synthase monomers, when fused into giant unilamellar vesicles (GUVs), forms voltage-gated and Ca2+-activated channels with the key features of mPTP. Based on our findings we conclude that the ATP synthase monomer is sufficient, and dimer formation is not required, for mPTP activity.

Date: 2019
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DOI: 10.1038/s41467-019-13766-2

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