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

TitleChannel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition.
Publication TypeJournal Article
Year of Publication2014
AuthorsCarraro, M, Giorgio, V, Šileikytė, J, Sartori, G, Forte, M, Lippe, G, Zoratti, M, Szabó, I, Bernardi, P
JournalJ Biol Chem
Volume289
Issue23
Pagination15980-5
Date Published2014 Jun 06
ISSN1083-351X
KeywordsBlotting, Western, Dimerization, Electrophoresis, Polyacrylamide Gel, Mitochondrial Membrane Transport Proteins, Mitochondrial Proton-Translocating ATPases, Saccharomyces cerevisiae
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 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.

DOI10.1074/jbc.C114.559633
Alternate JournalJ. Biol. Chem.
Citation Key10.1074/jbc.C114.559633
PubMed ID24790105
PubMed Central IDPMC4047373
Grant ListR01 GM069883 / GM / NIGMS NIH HHS / United States
1R01GM069883 / GM / NIGMS NIH HHS / United States