Abstract
The interaction of bovine heart mitochondrial oligomycin-sensitive ATPase (Serrano, R., Kranner, B. L., and Racker, E. (1976) J. Biol. Chem. 251, 2453-2461) with phospholipids has been examined by labeling the subunits exposed to lipids with photoreactive radioactive phospholipids. A subunit of Mr = 29,000 and some polypeptides in the range of 6,000 to 13,000 daltons were labeled. F1-ATPase subunits did not interact with the photoactive probes. This result is compared with the different pattern of labeling obtained with another mitochondrial ATPase preparation (Galante, Y.M., Wong, S. Y., and Hatefi, Y. (1979) J. Biol. Chem. 254, 12372-12378), which is devoid of the 29,000 component.
Highlights
The interaction of bovine heart mitochondrial oligomycin-sensitive ATPase
Upon illumination with nonprotein-damaging radiations, they bind covalently to their neighbor molecules. If they are next to a protein in the lipid bilayer, they cross-link to it, transforming a noncovalent relationship intoa stable covalentbond, which can be detected by SDS-polyacrylamide gel electrophoresis
An ATPase complex can be isolated from ATP-synthesizing approach on the interaction of bovine heart mitochondrial membranes such ams itochondrial [1,2,3,4,5], chloroplast [6],yeast OS-ATPase with a lipid bilayer
Summary
Its ATPase activity is inhibited by oligomycin and by N , N”dicyclohexy1carbodiimide andiits strongly dependent on thepresence of phospholipids. Vesicles of egg lecithin (0.675%, w/w, in 10 mM Tris/4-(2-hydroxyethyl)-l-piperazineethanesulfonic acid (Hepes) deaerated buffer, pH 7.4) were preweight of360000 and it can be resolved by SDS-polyacryl- pared by ultrasonic dispersion in a sonicating bath OS-ATPase was incubated with the phospholipid vesicles (3 pmol of lipid/mg of protein) for 1 h at mitochondrial inner membrane into the aqueous matrix spac4°eC and irradiatedwith a 100-watt ultravioleltamp The slices were incubated with a mixture of Lumasolve, Lipoluma, and water
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