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.
Highlights
Whether channel formation is a general feature of F-ATP synthase dimers across species is unknown
These results show that the yeast permeability transition pore (PTP) originates from F-ATP synthase and indicate that dimerization is required for pore formation in situ
Properties of the Ca2ϩ-dependent Permeability Transition of Yeast Mitochondria—We used ETH129 to allow Ca2ϩ uptake by energized yeast mitochondria [20] and monitored the propensity of the yeast PTP (yPTP) to open based on the Ca2ϩ retention capacity (CRC), i.e. the maximal Ca2ϩ load retained by mitochondria before onset of the permeability transition (PT) [22]
Summary
Whether channel formation is a general feature of F-ATP synthase dimers across species is unknown. Results: Yeast F-ATP synthase dimers form Ca2ϩ-dependent channels, and the e and g subunits facilitate pore formation in situ through dimerization.
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