Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition.
J Biol Chem
; 289(23): 15980-5, 2014 Jun 06.
Article
em En
| MEDLINE
| ID: mdl-24790105
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.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
/
ATPases Mitocondriais Próton-Translocadoras
/
Proteínas de Transporte da Membrana Mitocondrial
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2014
Tipo de documento:
Article