National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)
NS064967
United States
National Institutes of Health/National Institute on Aging (NIH/NIA)
K01AG054734
United States
Citation
Journal: Nat Commun / Year: 2019 Title: A mitochondrial megachannel resides in monomeric FF ATP synthase. Authors: Nelli Mnatsakanyan / Marc C Llaguno / Youshan Yang / Yangyang Yan / Joachim Weber / Fred J Sigworth / Elizabeth A Jonas / Abstract: Purified mitochondrial ATP synthase has been shown to form Ca-activated, large conductance channel activity similar to that of mitochondrial megachannel (MMC) or mitochondrial permeability transition ...Purified mitochondrial ATP synthase has been shown to form Ca-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 86 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 Ca-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.
History
Deposition
Nov 19, 2019
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Header (metadata) release
Dec 4, 2019
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Map release
Jan 1, 2020
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Update
Jan 1, 2020
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Current status
Jan 1, 2020
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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