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

doi:10.1074/jbc.C114.559633

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

Vollum Institute

Research output: Contribution to journal › Article › peer-review

127 Scopus citations

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 language	English (US)
Pages (from-to)	15980-15985
Number of pages	6
Journal	Journal of Biological Chemistry
Volume	289
Issue number	23
DOIs	https://doi.org/10.1074/jbc.C114.559633
State	Published - Jun 6 2014

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.C114.559633

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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.",

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AU - Carraro, Michela

AU - Giorgio, Valentina

AU - Sileikyte, Justina

AU - Sartori, Geppo

AU - Forte, Michael

AU - Lippe, Giovanna

AU - Zoratti, Mario

AU - Szabò, Ildikò

AU - Bernardi, Paolo

PY - 2014/6/6

Y1 - 2014/6/6

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AB - 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.

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

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