Spectral Tuning of Pigments Underlying Red-Green Color Vision

Neitz, Maureen; Neitz, Jay; Jacobs, Gerald H.

doi:10.1126/science.1903559

Cited by 465 publications

(322 citation statements)

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“…The same sites also account for the spectral shift between the red and green LWS pigments of primates ( Neitz et al 1991;Ibbotson et al 1992;Williams et al 1992) and are also substituted in the duplicated LWS genes of the blind cave fish, Astyanax ( Yokoyama & Yokoyama 1990). These are all examples of convergent evolution in distantly related species and confirm the assertion (Hunt et al 2001(Hunt et al , 2004) that in many cases spectral tuning of a visual pigment can only be achieved by substitution at a limited number of sites that are able to interact with the chromophore to achieve the spectral shift and maintain a fully functional pigment.…”

Section: Discussionmentioning

confidence: 99%

“…A duplicated LWS opsin gene underlies the red and green pigments in Old World primates (Dulai et al 1999) and the spectral shifts between these two pigments are largely attributable to substitutions at three sites, 180, 277 and 285, with polar residues Thr, Tyr and Thr, respectively, occupying these sites in the red pigment compared with non-polar residues Ala, Phe and Ala, respectively, in the green pigment ( Neitz et al 1991;Ibbotson et al 1992). Significantly, the honey possum and the fat-tailed dunnart also differ at sites 277 and 285, with polar Tyr and Thr in the more LW-shifted honey possum pigment.…”

Section: Resultsmentioning

confidence: 99%

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Cone visual pigments in two marsupial species: the fat-tailed dunnart (Sminthopsis crassicaudata) and the honey possum (Tarsipes rostratus)

Cowing¹,

Arrese²,

Davies

et al. 2008

Proc. R. Soc. B.

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Uniquely for non-primate mammals, three classes of cone photoreceptors have been previously identified by microspectrophotometry in two marsupial species: the polyprotodont fat-tailed dunnart (Sminthopsis crassicaudata) and the diprotodont honey possum (Tarsipes rostratus). This report focuses on the genetic basis for these three pigments. Two cone pigments were amplified from retinal cDNA of both species and identified by phylogenetics as members of the short wavelength-sensitive 1 (SWS1) and long wavelengthsensitive (LWS) opsin classes. In vitro expression of the two sequences from the fat-tailed dunnart confirmed the peak absorbances at 363 nm in the UV for the SWS1 pigment and 533 nm for the LWS pigment. No additional expressed cone opsin sequences that could account for the middle wavelength cones could be amplified. However, amplification from the fat-tailed dunnart genomic DNA with RH1 (rod) opsin primer pairs identified two genes with identical coding regions but sequence differences in introns 2 and 3. Uniquely therefore for a mammal, the fat-tailed dunnart has two copies of an RH1 opsin gene. This raises the possibility that the middle wavelength cones express a rod rather than a cone pigment.

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Section: Discussionmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Cone visual pigments in two marsupial species: the fat-tailed dunnart (Sminthopsis crassicaudata) and the honey possum (Tarsipes rostratus)

Cowing¹,

Arrese²,

Davies

et al. 2008

Proc. R. Soc. B.

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“…The clear variations in the pigments of the New World monkeys suggested it would be profitable to correlate spectral positioning with sequence differences among several different phenotypic versions of the M and L cone pigments in these animals. Accordingly, we made sequence comparisons for a total of eight different opsin genes, six from two species of New World monkey and two from human dichromats (44). The results indicated that as few as three amino acid substitutions were sufficient to explain the variations in the spectra of these pigments.…”

Section: Cone Photopigment Polymorphismmentioning

confidence: 99%

Primate photopigments and primate color vision.

Jacobs

1996

Proc. Natl. Acad. Sci. U.S.A.

234

128

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The past 15 years have brought much progress in our understanding of several basic features of primate color vision. There has been particular success in cataloging the spectral properties of the cone photopigments found in retinas of a number of primate species and in elucidating the relationship between cone opsin genes and their photopigment products. Direct studies of color vision show that there are several modal patterns of color vision among groupings of primates: (i) Old World monkeys, apes, and humans all enjoy trichromatic color vision, although the former two groups do not seem prone to the polymorphic variations in color vision that are characteristic of people; (ii) most species of New World monkeys are highly polymorphic, with individual animals having any of several types of dichromatic or trichromatic color vision; (iii) less is known about color vision in prosimians, but evidence suggests that at least some diurnal species have dichromatic color vision; and (iv) some nocturnal primates may lack color vision completely. In many cases the photopigments and photopigment gene arrangements underlying these patterns have been revealed and, as a result, hints are emerging about the evolution of color vision among the primates.The generalization that color vision is a more developed and acute capacity in primates than it is in other mammals came from a consideration of the natural history of mammals (1). There is now extensive experimental support for this proposition (2), but a surprise from the results of color-vision studies of the past two decades is that primate color vision is not monolithic. The substantial variations in color vision that have been revealed, both among the members of some species of primate and between various groupings of species, have provided the opportunity to examine in greater detail the biological mechanisms that underlie color vision, particularly the photopigments of cone photoreceptors and the genes crucial for the production of these photopigments. These findings also provide leads about the evolution of primate color vision, and they have served to reawaken interest in understanding the functional utility of color vision. Cone Photopigment PolymorphismThe biological process that results in color vision is initiated by the neural comparison of signals from classes of cone photoreceptor that contain spectrally distinct photopigments. Among other things, the nature of the color vision that ensues depends on the number of such classes of photopigment, the spectral separation of the photopigments, and the relative representation of the different pigments among the population of photoreceptors. An elegant feature of color vision is thatThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.variations in the number of types of cone pigment found in the retina normally map directly into the dimensionality of color vi...

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“…In contrast, the NPXXY region is highly homologous among cone pigments and rhodopsin (data not shown). The only difference in the chromophore-binding site between green and red pigments is in the immediate vicinity of retinal, where Phe 261 is replaced by Tyr 261 (red), as predicted from studies on the spectral tuning of primates aimed at understanding the molecular properties underlying red-green color vision (155,156). These studies were extended to identify residues responsible in in vitro experiments [157, 158; reviewed in (159)].…”

Section: Cone Visual Pigmentsmentioning

confidence: 99%

G Protein-Coupled Receptor Rhodopsin: A Prospectus

Filipek

Stenkamp

Teller

et al. 2003

Annu. Rev. Physiol.

227

196

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Rhodopsin is a retinal photoreceptor protein of bipartite structure consisting of the transmembrane protein opsin and a light-sensitive chromophore 11-cis-retinal, linked to opsin via a protonated Schiff base. Studies on rhodopsin have unveiled many structural and functional features that are common to a large and pharmacologically important group of proteins from the G protein-coupled receptor (GPCR) superfamily, of which rhodopsin is the best-studied member. In this work, we focus on structural features of rhodopsin as revealed by many biochemical and structural investigations. In particular, the high-resolution structure of bovine rhodopsin provides a template for understanding how GPCRs work. We describe the sensitivity and complexity of rhodopsin that lead to its important role in vision.

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Spectral Tuning of Pigments Underlying Red-Green Color Vision

Cited by 465 publications

References 14 publications

Cone visual pigments in two marsupial species: the fat-tailed dunnart (Sminthopsis crassicaudata) and the honey possum (Tarsipes rostratus)

Cone visual pigments in two marsupial species: the fat-tailed dunnart (Sminthopsis crassicaudata) and the honey possum (Tarsipes rostratus)

Primate photopigments and primate color vision.

G Protein-Coupled Receptor Rhodopsin: A Prospectus

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