title: Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria.
abstract: ATP synthase, or F-ATPase, purified from bovine heart mitochondria in the absence of phospholipids is an assembly of 16 different subunits. In the presence of exogenous phospholipids, two additional hydrophobic proteins, a 6.8kDa proteolipid and diabetes associated protein in insulin sensitive tissue (DAPIT), were associated with the purified complex, with DAPIT at sub-stoichiometric levels. Both proteins are conserved in vertebrates and invertebrates, but not in fungi, and prokaryotic F-ATPases do not contain orthologues of either of them. Therefore, their roles are likely to be peripheral to the synthesis of ATP.
authors.affiliation: Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge, UK.
authors.forename: Ruming
authors.initials: R
authors.lastname: Chen
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Runswick
authors.forename: Joe
authors.initials: J
authors.lastname: Carroll
authors.forename: Ian M
authors.initials: IM
authors.lastname: Fearnley
authors.forename: John E
authors.initials: JE
authors.lastname: Walker
mesh_terms: D000818:Animals; D002417:Cattle; D008565:Membrane Proteins / Q000378:metabolism; D008929:Mitochondria, Heart / Q000201:enzymology* / Q000378:metabolism; D025261:Mitochondrial Proton-Translocating ATPases / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding; D011510:Proteolipids / Q000302:isolation & purification / Q000378:metabolism* / Q000502:physiology*
chemical_list: D008565:Membrane Proteins; D011510:Proteolipids; D025261:Mitochondrial Proton-Translocating ATPases