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

FEBS Lett. 2007 Jul 10;581(17):3145-8. doi: 10.1016/j.febslet.2007.05.079. Epub 2007 Jun 8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Membrane Proteins / metabolism
  • Mitochondria, Heart / enzymology*
  • Mitochondria, Heart / metabolism
  • Mitochondrial Proton-Translocating ATPases / isolation & purification
  • Mitochondrial Proton-Translocating ATPases / metabolism*
  • Protein Binding
  • Proteolipids / isolation & purification
  • Proteolipids / metabolism*
  • Proteolipids / physiology*

Substances

  • Membrane Proteins
  • Proteolipids
  • Mitochondrial Proton-Translocating ATPases