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

TitleAssociation of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria.
Publication TypeJournal Article
Year of Publication2007
AuthorsChen, R, Runswick, MJ, Carroll, J, Fearnley, IM, Walker, JE
JournalFEBS Lett
Volume581
Issue17
Pagination3145-8
Date Published2007 Jul 10
ISSN0014-5793
KeywordsAnimals, Cattle, Membrane Proteins, Mitochondria, Heart, Mitochondrial Proton-Translocating ATPases, Protein Binding, Proteolipids
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.

DOI10.1016/j.febslet.2007.05.079
Alternate JournalFEBS Lett.
Citation Key10.1016/j.febslet.2007.05.079
PubMed ID17570365
Grant ListMC_U105663148 / / Medical Research Council / United Kingdom