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 6.8 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.
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Dates
Type | When |
---|---|
Created | 18 years, 2 months ago (June 11, 2007, 9:04 a.m.) |
Deposited | 1 year, 10 months ago (Oct. 12, 2023, 5:57 p.m.) |
Indexed | 1 year ago (Aug. 5, 2024, 5:50 a.m.) |
Issued | 18 years, 2 months ago (June 8, 2007) |
Published | 18 years, 2 months ago (June 8, 2007) |
Published Online | 18 years, 2 months ago (June 8, 2007) |
Published Print | 18 years, 1 month ago (July 10, 2007) |
@article{Chen_2007, title={Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria}, volume={581}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/j.febslet.2007.05.079}, DOI={10.1016/j.febslet.2007.05.079}, number={17}, journal={FEBS Letters}, publisher={Wiley}, author={Chen, Ruming and Runswick, Michael J. and Carroll, Joe and Fearnley, Ian M. and Walker, John E.}, year={2007}, month=jun, pages={3145–3148} }