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J. Biol. Chem., Vol. 281, Issue 44, 33233-33241, November 3, 2006

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Evidence for Specificity in Lipid-Rhodopsin Interactions^*

From the Laboratory of Membrane Biochemistry and Biophysics, NIAAA, National Institutes of Health, Bethesda, Maryland 20892

The interaction of bovine rhodopsin with poly- and monounsaturated lipids was studied by ¹H MAS NMR with magnetization transfer from rhodopsin to lipid. Experiments were conducted on bovine rod outer segment (ROS) disks and on recombinant membranes containing lipids with polyunsaturated, docosahexaenoyl (DHA) chains. Poly- and monounsaturated lipids interact specifically with different sites on the rhodopsin surface. Rates of magnetization transfer from protein to DHA are lipid headgroup-dependent and increased in the sequence PC < PS < PE. Boundary lipids are in fast exchange with the lipid matrix on a time scale of milliseconds or shorter. All rhodopsin photointermediates transferred magnetization preferentially to DHA-containing lipids, but highest rates were observed for Meta-III rhodopsin. The experiments show clearly that the surface of rhodopsin has sites for specific interaction with lipids. Current theories of lipid-protein interaction do not account for such surface heterogeneity.

Received for publication, March 31, 2006 , and in revised form, September 6, 2006.

^* This work was supported by the Intramural Research Program of NIAAA, National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: NMR Section, Laboratory of Membrane Biochemistry and Biophysics, NIAAA, National Institutes of Health, 5625 Fishers Lane, Bethesda, MD 20892-9410. Tel.: 301-594-3750; Fax: 301-594-0035; E-mail: gawrisch{at}helix.nih.gov.

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