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FEBS Lett. 2007 Jul 10;581(17):3145-8. Epub 2007 Jun 8.

Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria.

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Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge, UK.


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.

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