Reports
Channel Formation by Yeast F-ATP Synthase and the Role of Dimerization in the Mitochondrial Permeability Transition*♦

https://doi.org/10.1074/jbc.C114.559633Get rights and content
Under a Creative Commons license
open access

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.

Calcium
F1FO-ATPase
Ion Channel
Mitochondria
Mitochondrial Permeability Transition (MPT)
Oxidative Stress
Yeast

Cited by (0)

*

This work was supported in part by Associazione Italiana per la Ricerca sul Cancro (AIRC) Grants IG13392 (to P. B.) and IG11814 (to I. S.), Progetti di Ricerca di Interesse Nazionale Programs 20107Z8XBW (to P. B.) and 2010CSJX4F (to I. S.), National Institutes of Health/Public Health Service Grant 1R01GM069883 (to M. F. and P. B.), a Consiglio Nazionale delle Ricerche (CNR) Project of Special Interest on Aging (to M. Z.), and the University of Padova Progetti Strategici di Ateneo ”Models of Mitochondrial Diseases“ (to P. B.).

♦

This article was selected as a Paper of the Week.

1

Both authors contributed equally to this work.

2

This work is in partial fulfillment of the requirements for a Ph.D. at the University of Padova.

© 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.