|Title||Two ATP synthases can be linked through subunits i in the inner mitochondrial membrane of Saccharomyces cerevisiae.|
|Publication Type||Journal Article|
|Year of Publication||2002|
|Authors||Paumard, P, Arselin, G, Vaillier, J, Chaignepain, S, Bathany, K, Schmitter, JMarie, Brèthes, D, Velours, J|
|Date Published||2002 Aug 20|
|Keywords||Amino Acid Sequence, Cross-Linking Reagents, Dimerization, Intracellular Membranes, Maleimides, Mitochondria, Mitochondrial Proton-Translocating ATPases, Molecular Sequence Data, Proton-Translocating ATPases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins|
Cross-linking experiments showed that the supernumerary subunit i is close to the interface between two ATP synthases. These data were used to demonstrate the presence of ATP synthase dimers in the inner mitochondrial membrane of Saccharomyces cerevisiae. A cysteine residue was introduced into the inter-membrane space located C-terminal part of subunit i. Cross-linking experiments revealed a dimerization of subunit i. This cross-linking occurred only with the dimeric form of the enzyme after incubating intact mitochondria with a bis-maleimide reagent, thus indicating an inter-ATP synthase cross-linking, whereas the monomeric form of the enzyme exhibited only an intra-ATP synthase cross-linking with subunit 6, another component of the membranous domain of the ATP synthase.