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J. Biol. Chem., Vol. 267, Issue 24, 16889-16894, Aug, 1992
DI Papac, KR Thornburg, EE Bullesbach, RK Crouch and DR Knapp
Bovine rhodopsin has been reported to be S-palmitylated at cysteines 322
and 323 (Ovchinnikov, Y. A., Abdulaev, N. G., and Bogachuk, A.S. (1988)
FEBS Lett. 230, 1-5). Using a combination of enzymatic and chemical
cleavage techniques in conjunction with tandem mass spectrometry, the sites
of incorporation of the palmityl groups are shown. Bovine rhodopsin in disc
membranes was digested with thermolysin to generate the C-terminal fragment
(241-327), which was subsequently cleaved with cyanogen bromide to generate
the peptide Val-Thr-Thr-Leu- Cys-Cys-Gly-Lys-Asn-Pro (318-327). A
bis-S-palmitylated synthetic standard had the same retention time by
reversed-phase high performance liquid chromatography as the isolated
peptide and the same molecular weight (MH+1511.7) by liquid secondary ion
mass spectrometry. Dithiothreitol reduction of both the isolated and the
synthetic peptide cleaved the two thioester-linked palmityl groups to
produce reduction products of the same appropriately decreased molecular
weight (MH+1035.5). Tandem mass spectrometry of the isolated and the
synthetic peptide identified the sites of attachment of the palmityl groups
on cysteines 322 and 323. These results prove the modification of cysteines
322 and 323 with palmitic acid in bovine rhodopsin, and illustrate the
utility of mass spectrometry to characterize the post- translational
modifications in G-protein coupled receptors.
Palmitylation of a G-protein coupled receptor. Direct analysis by tandem mass spectrometry
Department of Cell and Molecular Pharmacology, Medical University of South Carolina, Charleston 29425.
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