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J. Biol. Chem., Vol. 262, Issue 11, 5210-5215, 04, 1987
PJ O'Brien, RS St. Jules, TS Reddy, NG Bazan and M Zatz
Bovine retinal rod outer segments (ROS) support the incorporation of
[3H]palmitate into rhodopsin. [14C] Palmitoyl-CoA serves as the donor with
an apparent Km of 40 microM. Solubilization of ROS in the detergent,
Emulphogene, results in increased incorporation of label into rhodopsin. A
further increase is found when ConA-Sepharose- purified rhodopsin is used
as the source of both "enzyme" and acceptor. Failure to separate enzyme
from acceptor suggested the possibility of a nonenzymatic reaction. This
was confirmed when boiled rhodopsin was found to support the reaction.
However, the acylation of rhodopsin is not an artifact since analysis of
purified native rhodopsin reveals the presence of covalently bound
palmitate and we showed that whole bovine retinas incubated with [3H]
palmitate incorporated the fatty acid into rhodopsin (O'Brien, P.J., and
Zatz, M. (1984) J. Biol. Chem. 259, 5054- 5057). Furthermore, in vivo
experiments with rat retinas have revealed that opsin is acylated both in
the rod inner and outer segments (St. Jules, R. S., and O'Brien, P.J.
(1986) Exp. Eye Res. 43, 929-940). Incubation of labeled rhodopsin with
mercaptoethanol resulted in release of the labeled palmitate indicating the
presence of a thioester bond. This also illustrates the ease with which a
thioester, such as palmitoyl cysteine or palmitoyl-CoA, can transfer the
fatty acyl group to a free thiol, such as cysteine or mercaptoethanol.
Acylation of disc membrane rhodopsin may be nonenzymatic
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