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(Received for publication, March 7, 1996, and in revised form, May 14, 1996)
From the Departments of Rhodopsin is constrained in an inactive
conformation by interactions with 11-cis-retinal including
formation of a protonated Schiff base with Lys296. Upon
photoisomerization, major structural rearrangements that involve
protonation of the active site Glu113 and cytoplasmic
acidic residues, including Glu134, lead to the formation of
the active form of the receptor, metarhodopsin II b, which decays to
opsin. However, an activated receptor may be generated without
illumination by addition of all-trans-retinal or its
analogues to opsin, as measured in this study by the increased
phosphorylation of opsin by rhodopsin kinase. The potency of
stimulation depended on the chemical and isomeric nature of the
analogues and the length of the polyene chain with
all-trans-C17 aldehyde and all-trans-retinal
being the most active and trans-C12 aldehyde being the
least active. Certain cis-isomers,
11-cis-13-demethyl-retinal and 9-cis-C17
aldehyde, were also active. Most of the retinal analogues tested did
not regenerate a spectrally identifiable pigment, and many were
incapable of Schiff base formation (ketone, stable oximes, and Schiff
base-derivatives of retinal). Thus, receptor activation resulted from
formation of non-covalent complexes with opsin. pH titrations suggested
that an equilibrium exists between partially active (protonated) and
inactive (deprotonated) forms of opsin. These findings are
consistent with a model in which protonation of one or more cytoplasmic
carboxyl groups of opsin is essential for activity. Upon addition of
retinoids, the partially active conformation of opsin is converted to a
more active intermediate similar to metarhodopsin II b. The model
provides an understanding of the structural requirements for opsin
activation and an interpretation of the observed activities of natural
and experimental opsin mutants.
Volume 271, Number 34,
Issue of August 23, 1996
pp. 20621-20630
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
ko
,§
,
and''
Ophthalmology,
§ Biochemistry, and '' Pharmacology, School of Medicine,
University of Washington, Seattle, Washington 98195 and the
Department of Ophthalmology, Medical University of South
Carolina, Charleston, South Carolina 29425
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