Association of Two Proteolipids of Unknown Function with Atp Synthase from Bovine Heart Mitochondria.
From: Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge, UK.
FEBS letters
- Publish Date: Jul 2007
- ISSN: 0014-5793
- Volume: 581
- Issue: 17
- Pages: 3145-8
- Medium: Print
- Language: English
- Citation (JAMA): Chen Ruming, Runswick Michael J, Carroll Joe, et al. Association of Two Proteolipids of Unknown Function with Atp Synthase from Bovine Heart Mitochondria.. FEBS Lett. Jul 2007;581:3145-8
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.
Mesh Headings (Keywords): Animals, Cattle, Membrane Proteins, Mitochondria, Heart, Mitochondrial Proton-Translocating ATPases, Protein Binding, Proteolipids
Check for Full Text / PubMed Unique Identifier (PMID): 17570365
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