| Literature DB >> 17570365 |
Ruming Chen1, Michael J Runswick, Joe Carroll, Ian M Fearnley, John E Walker.
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.Entities:
Mesh：
Substances：
Year: 2007 PMID： 17570365 DOI： 10.1016/j.febslet.2007.05.079
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124