Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition

Michela Carraro, Valentina Giorgio, Justina Sileikyte, Geppo Sartori, Michael Forte, Giovanna Lippe, Mario Zoratti, Ildikò Szabò, Paolo Bernardi

Research output: Contribution to journalArticle

Abstract

Purified F-ATP synthase dimers of yeast mitochondria display Ca 2+-dependent channel activity with properties resembling those of the permeability transition pore (PTP) of mammals. After treatment with the Ca 2+ ionophore ETH129, which allows electrophoretic Ca2+ uptake, isolated yeast mitochondria undergo inner membrane permeabilization due to PTP opening. Yeast mutant strains ATIM11 and AATP20 (lacking the e and g F-ATP synthase subunits, respectively, which are necessary for dimer formation) display a striking resistance to PTP opening. These results show that the yeast PTP originates from F-ATP synthase and indicate that dimerization is required for pore formation in situ.

Original languageEnglish (US)
Pages (from-to)15980-15985
Number of pages6
JournalJournal of Biological Chemistry
Volume289
Issue number23
DOIs
StatePublished - Jun 6 2014

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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  • Cite this

    Carraro, M., Giorgio, V., Sileikyte, J., Sartori, G., Forte, M., Lippe, G., Zoratti, M., Szabò, I., & Bernardi, P. (2014). Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition. Journal of Biological Chemistry, 289(23), 15980-15985. https://doi.org/10.1074/jbcC114.559633