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Volume 270, Number 12, Issue of March 24, 1995 pp. 6718-6721
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Reduced Light-dependent Phosphorylation of an Analog Visual Pigment Containing 9-Demethylretinal as Its Chromophore (*)

(Received for publication, October 20, 1994)

Daniel F. Morrison (1),  Tuow D. Ting (2),  Visalakshi Vallury (1),  (2),  Yee-Kin Ho (2),  Rosalie K. Crouch (3),  D. Wesley Corson (3),  (4),  Nancy J. Mangini (1),  David R. Pepperberg (1)(§)

From the  (1)Lions of Illinois Eye Research Institute, Department of Ophthalmology and Visual Sciences and the (2)Department of Biochemistry, University of Illinois at Chicago College of Medicine, Chicago, Illinois 60612 and the (3)Departments of Ophthalmology and (4)Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston, South Carolina 29425

ABSTRACT

9-Demethyl rhodopsin (9dR), an analog of vertebrate rhodopsin, consists of opsin and a covalently attached chromophore of 11-cis 9-demethylretinal. Electrophysiological evidence that photoactivated 9dR (9dR*) undergoes abnormally slow deactivation in salamander rods (Corson, D. W., Cornwall, M. C., and Pepperberg, D. R.(1994) Visual Neurosci. 11, 91-98) raises the possibility that opsin phosphorylation, a reaction involved in visual pigment deactivation, operates abnormally on 9dR*. This possibility was tested by measuring the light-dependent phosphorylation of 9dR in preparations obtained from bovine rod outer segments. Outer segment membranes containing 9dR or regenerated rhodopsin were flash-illuminated in the presence of [-P]ATP and rhodopsin kinase, further incubated in darkness, and then analyzed for opsin-bound [P]P(i). [P]P(i) incorporation by 9dR* increased with both incubation period and bleaching extent but, under all conditions tested, was less than that measured in rhodopsin controls. Results obtained with 30-s incubation periods indicated that the maximal initial rate of incorporation by 9dR* is about 25% of that by photoactivated rhodopsin. The results imply that the low incorporation of P(i) by 9dR* results from a reduced rate of phosphorylation by rhodopsin kinase and are consistent with the prolonged lifetime of 9dR* determined electrophysiologically.

FOOTNOTES

*
This research was supported by Grants EY-06038, EY-05494, EY-01792, EY-05788, EY-04939, EY-07543, and EY-07586 from NEI, National Institutes of Health; by unrestricted grants from Research to Prevent Blindness, Inc.; by the Lions of Illinois Foundation, Maywood, Illinois; and by the Illinois Eye Fund. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked ``advertisement'' in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§
To whom correspondence should be addressed: Dept. of Ophthalmology and Visual Sciences, University of Illinois at Chicago, 1855 W. Taylor St., Chicago, IL 60612, Tel.: 312-996-4262.

(^1)
The abbreviations used are: R*, photoactivated rhodopsin; 9dR, 9-demethyl rhodopsin; 9dR*, photoactivated 9-demethyl rhodopsin; ROS, rod outer segments; BTP, 1,3-bis[tris(hydroxymethyl)methylamino]propane.

ACKNOWLEDGEMENTS

We are grateful to Dr. F. Derguini, Dr. K. Nakanishi, and the late P. K. Brown for gifts of 11-cis 9-demethylretinal and 11-cis retinal. We also thank Drs. K. P. Hofmann, K. Palczewski, and T.-I. L. Okajima for helpful discussions.

©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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