Journal
FEBS LETTERS
Volume 581, Issue 17, Pages 3145-3148Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.05.079
Keywords
mitochondria; ATP synthase; 6.8 kDa proteolipid; DAPIT; subunit composition
Funding
- Medical Research Council [MC_U105663148] Funding Source: Medline
- Medical Research Council [MC_U105663148] Funding Source: researchfish
- MRC [MC_U105663148] Funding Source: UKRI
Ask authors/readers for more resources
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 6.8 kDa 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. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available