Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria.
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.
Chen
Ruming
R
Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge, UK.
Runswick
Michael J
MJ
Carroll
Joe
J
Fearnley
Ian M
IM
Walker
John E
JE
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*
D008565:Membrane Proteins; D011510:Proteolipids; D025261:Mitochondrial Proton-Translocating ATPases