Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition.
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 Ca(2+) 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.
From the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Michela
M
Carraro
From the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Valentina
V
Giorgio
From the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Justina
J
Šileikytė
From the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Geppo
G
Sartori
the Vollum Institute, Oregon Health and Sciences University, Portland, Oregon 97239-3098, and.
Michael
M
Forte
the Department of Food Science, University of Udine, 33100 Udine, Italy.
Giovanna
G
Lippe
From the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Mario
M
Zoratti
the Department of Biology, University of Padova, I-35121 Padova, Italy.
Ildikò
I
Szabò
From the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and bernardi@bio.unipd.it.
Paolo
P
Bernardi
D015153:Blotting, Western; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D033681:Mitochondrial Membrane Transport Proteins / Q000737:chemistry / Q000502:physiology*; D000083162:Mitochondrial Permeability Transition Pore; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D033681:Mitochondrial Membrane Transport Proteins; D000083162:Mitochondrial Permeability Transition Pore; D025261:Mitochondrial Proton-Translocating ATPases
Calcium; F1FO-ATPase; Ion Channel; Mitochondria; Mitochondrial Permeability Transition (MPT); Oxidative Stress; Yeast