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TitleA mitochondrial megachannel resides in monomeric FF ATP synthase.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 5823, Year 2019
Publish dateDec 20, 2019
AuthorsNelli Mnatsakanyan / Marc C Llaguno / Youshan Yang / Yangyang Yan / Joachim Weber / Fred J Sigworth / Elizabeth A Jonas /
PubMed AbstractPurified 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.
External linksNat Commun / PubMed:31862883 / PubMed Central
MethodsEM (single particle)
Resolution19.0 - 30.0 Å
Structure data

EMDB-21001:
Cryo-EM structure of porcine ATP synthase reconstituted in small unilamellar vesicles_I
Method: EM (single particle) / Resolution: 19.0 Å

EMDB-21002:
Cryo-EM structure of porcine ATP synthase reconstituted in small unilamellar vesicles_II
Method: EM (single particle) / Resolution: 30.0 Å

Source
  • Sus scrofa (pig)

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