Evidence of the proximity of ATP synthase subunits 6(a) in the inner mitochondrial membrane and in the supramolecular forms of Saccharomyces cerevisiae ATP synthase - Archive ouverte HAL Access content directly
Journal Articles Journal of Biological Chemistry Year : 2011

Evidence of the proximity of ATP synthase subunits 6(a) in the inner mitochondrial membrane and in the supramolecular forms of Saccharomyces cerevisiae ATP synthase

Abstract

The involvement of subunit 6 (a) in the interface between yeast ATP synthase monomers has been highlighted. Based on the formation of a disulfide bond and using the unique cysteine 23 as target, we show that two subunits 6 are close in the inner mitochondrial membrane and in the solubilized supramolecular forms of the yeast ATP synthase. In a null mutant devoid of supernumerary subunits e and g that are involved in the stabilization of ATP synthase dimers, ATP synthase monomers are close enough in the inner mitochondrial membrane to make a disulfide bridge between their subunits 6, and this proximity is maintained in detergent extract containing this enzyme. The cross-linking of cysteine 23 located in the N-terminal part of the first transmembrane helix of subunit 6 suggests that this membrane-spanning segment is in contact with its counterpart belonging to the ATP synthase monomer that faces it and participates in the monomer-monomer interface.

Dates and versions

hal-00637694 , version 1 (02-11-2011)

Identifiers

Cite

J. Velours, C. Stines-Chaumeil, J. Habersetzer, S. Chaignepain, A. Dautant, et al.. Evidence of the proximity of ATP synthase subunits 6(a) in the inner mitochondrial membrane and in the supramolecular forms of Saccharomyces cerevisiae ATP synthase. Journal of Biological Chemistry, 2011, 286 (41), pp.35477-84. ⟨10.1074/jbc.M111.275776⟩. ⟨hal-00637694⟩

Collections

CNRS
15 View
0 Download

Altmetric

Share

Gmail Facebook X LinkedIn More