Mechanism of spectral tuning in the dolphin visual pigments

The absorption maxima of both rod and cone visual pigments of the bottlenose dolphin (Tursiops truncatus) are blue-shifted relative to those of terrestrial mammals. A comparison of the sequence of the dolphin rod photopigment gene with that of the bovine rod suggests that, of the 28 nonidentical amino acids, three amino acid substitutions at positions 83, 292, and 299 in the dolphin rod pigment are responsible for the 10 nm blue shift in absorption maxima. A similar comparison of the dolphin long-wavelength sensitive (LWS) cone photopigment gene with those of the human LWS cones suggests that a single substitution at position 292 (using the convention of rhodopsin numbering) in the dolphin LWS cone pigment results in a blue shift in absorption maxima. A mutagenesis study reveals that the combination of the three dolphin specific substitutions in the bovine rod pigment (D-83 to N-83, (292)A to S-292,and (299)A to S-299) causes a blue shift from the wild-type lambda(max) of 499 nm to 489 nm. The single substitution in the dolphin LWS cone pigment (S-292 to (292)A) causes a red shift from the wild-type lambda(max) of 524 nm to 552 nm. The interactions of the three amino acids identified in the rod pigment with the chromophore may be a general mechanism for blue shifting in rod visual pigments. Furthermore, the single substitution in the dolphin LWS opsin gene is a novel mechanism of wavelength modulation in mammalian LWS pigments.