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. © 2014 by The American Society for Biochemistry and Molecular Biology.

Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition / Carraro M.; Giorgio V.; Sileikyte J.; Sartori G.; Forte M.; Lippe G.; Zoratti M.; Szabo I.; Bernardi P.. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - ELETTRONICO. - 289:23(2014), pp. 15980-15985. [10.1074/jbc.C114.559633]

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

Giorgio V.
Primo
;
2014

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. © 2014 by The American Society for Biochemistry and Molecular Biology.
2014
Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition / Carraro M.; Giorgio V.; Sileikyte J.; Sartori G.; Forte M.; Lippe G.; Zoratti M.; Szabo I.; Bernardi P.. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - ELETTRONICO. - 289:23(2014), pp. 15980-15985. [10.1074/jbc.C114.559633]
Carraro M.; Giorgio V.; Sileikyte J.; Sartori G.; Forte M.; Lippe G.; Zoratti M.; Szabo I.; Bernardi P.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/794376
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