Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition |
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| Authors: | Michela Carraro Valentina Giorgio Justina ?ileikyt? Geppo Sartori Michael Forte Giovanna Lippe Mario Zoratti Ildikò Szabò Paolo Bernardi |
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| Affiliation: | From the ‡Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and ;the ‖Department of Biology, University of Padova, I-35121 Padova, Italy ;the §Vollum Institute, Oregon Health and Sciences University, Portland, Oregon 97239-3098, and ;the ¶Department of Food Science, University of Udine, 33100 Udine, Italy |
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| Abstract: | Purified F-ATP synthase dimers of yeast mitochondria display Ca2+-dependent channel activity with properties resembling those of the permeability transition pore (PTP) of mammals. After treatment with the Ca2+ ionophore ETH129, which allows electrophoretic Ca2+ uptake, isolated yeast mitochondria undergo inner membrane permeabilization due to PTP opening. Yeast mutant strains ΔTIM11 and ΔATP20 (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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| Keywords: | Calcium F1FO-ATPase Ion Channel Mitochondria Mitochondrial Permeability Transition (MPT) Oxidative Stress Yeast |
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