期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 289, 期 23, 页码 15980-15985出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C114.559633
关键词
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资金
- Associazione Italiana per la Ricerca sul Cancro (AIRC) [IG13392, IG11814]
- Progetti di Ricerca di Interesse Nazionale Programs [20107Z8XBW, 2010CSJX4F]
- National Institutes of Health/Public Health Service Grant [1R01GM069883]
- Consiglio Nazionale delle Ricerche (CNR) Project of Special Interest on Aging
- University of Padova Progetti Strategici di Ateneo Models of Mitochondrial Diseases
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 Delta TIM11 and Delta ATP20 (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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