Author： Zanotti Franco Raho Gabriella Gaballo Antonio Papa Sergio
Publisher： Springer Publishing Company
ISSN： 0145-479X
Source： Journal of Bioenergetics and Biomembranes, Vol.36, Iss.5, 2004-10, pp. : 447-457
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
The inhibitor protein IF1 is a basic protein of 84 residues which inhibits the ATPase activity of the mitochondrial FoF1-ATP synthase complex without having any effect on ATP synthesis. Results of cross-linking and limited proteolysis experiments are presented showing that in the intact FoF1 complex “in situ,” in the inner membrane of bovine heart mitochondria, the central segment of IF1 (residues 42–58) binds to the α and β subunits of F1 in a pH dependent process, and inhibits the ATPase activity. The C-terminal region of IF1 binds, simultaneously, to the OSCP subunit of Fo in a pH-independent process. This binding keeps IF1 anchored to the complex, both under inhibitory conditions, at acidic pH, and noninhibitory conditions at alkaline pH.
Related content
Access to resources
Recommend
By Bravo Concepción Minauro-Sanmiguel Fernando Morales-Ríos Edgar Rodríguez-Zavala José S. García José J.
Journal of Bioenergetics and Biomembranes, Vol. 36, Iss. 3, 2004-06 ,pp. :
By Gordon-Smith D.J. Carbajo R.J. Yang J-C. Videler H. Runswick M.J. Walker J.E. Neuhaus D.
Journal of Molecular Biology, Vol. 308, Iss. 2, 2001-04 ,pp. :