The origins of colour vision in vertebrates
- BiologyClinical & experimental optometry
Findings reveal that multiple opsin genes originated very early in vertebrate evolution, prior to the separation of the jawed and jawless vertebrate lineages, thereby providing the genetic basis for colour vision in all vertebrates.
A novel Xenopus SWS2, P434 visual pigment: structure, cellular location, and spectral analyses.
- BiologyMolecular vision
A novel green rod opsin cDNA has been cloned and sequenced from the retina of adult Xenopus laevis, which encodes a protein belonging to the SWS2 group of opsins, although it was identified only in the Xenopus green rod cells.
Molecular ecology and adaptation of visual photopigments in craniates
- BiologyMolecular ecology
This review discusses the origins and spectral tuning of photopigments that first arose in the agnathans to sample light within the ancient aquatic landscape of the Early Cambrian, detailing the molecular changes that subsequently occurred in each of the opsin classes independently within the main branches of extant jawed gnathostomes.
High molecular diversity in the rhodopsin gene in closely related goby fishes: A role for visual pigments in adaptive speciation?
- BiologyMolecular phylogenetics and evolution
Ancient colour vision: multiple opsin genes in the ancestral vertebrates
- BiologyCurrent Biology
The molecular genetics and evolution of red and green color vision in vertebrates.
Multiple regression analyses of ancestral and contemporary MWS and LWS pigments show that single mutations S180A, H197Y, Y277F, T285A, A308S, and double mutations S 180A/H197Y shift the lambda(max) of the pigments by -7, -28, -8, -15, -27, and 11 nm, respectively.
Molecular and Functional Diversity of Visual Pigments: Clues from the Photosensitive Opsin-Like Proteins of the Animal Model Hydra
The cnidarian Hydra, the first metazoan owning a nervous system, is proposed as a powerful tool of investigation to study molecular and functional differences between these pigment families, giving new insights on the molecular biology of Hydra photoreception and on comparative physiology of visual pigments.
Gene duplication and differential gene expression play an important role in the diversification of visual pigments in fish.
- BiologyIntegrative and comparative biology
The role that opsin duplication and differential gene expression have played in the diversification of visual pigments is reviewed and the findings in cichlids are compared to five other taxonomic groups to highlight the ways that their similarities and differences may provide new insights into the molecular genetic basis of sensory adaptation and diversification.
SHOWING 1-10 OF 195 REFERENCES
Molecular genetic basis of adaptive selection: examples from color vision in vertebrates.
- BiologyAnnual review of genetics
The identification of potentially important amino acid changes of pigments that are potentially important in changing the wavelength of maximal absorption (lambda max) are identified using evolutionary biological means and the effects of these mutations on the shift in lambda max are determined.
ADAPTIVE EVOLUTION OF PHOTORECEPTORS AND VISUAL PIGMENTS IN VERTEBRATES
Thanks to the molecular characterization of the opsin genes, it is now possible to study the types of opsins associated with certain environmental conditions, and these surveys will provide important first molecular clues to how animals adapt to their environments with respect to their coloration and behavior.
Phylogenetic analysis and experimental approaches to study color vision in vertebrates.
- BiologyMethods in enzymology
Molecular bases of color vision in vertebrates.
- BiologyGenes & genetic systems
A large number of amino acid changes have been introduced into the bovine rod-specific visual pigment (rhodopsin) by several groups of vision scientists and it is not immediately clear how these mutagenesis results are helpful in elucidating the molecular basis for the divergence of λmax values of visual pigments in nature.
Ectopic expression of ultraviolet-rhodopsins in the blue photoreceptor cells of Drosophila: visual physiology and photochemistry of transgenic animals
- BiologyThe Journal of neuroscience : the official journal of the Society for Neuroscience
It is shown that it is possible to coexpress two different visual pigments functionally in the same cell and produce photoreceptors that display the summed spectral response of the individual pigments.
The molecular basis for UV vision in birds: spectral characteristics, cDNA sequence and retinal localization of the UV-sensitive visual pigment of the budgerigar (Melopsittacus undulatus).
- BiologyThe Biochemical journal
This is the first UV opsin from an avian species to be sequenced and expressed in a heterologous system and yielded an absorption spectrum typical of a UV photopigment, with lambdamax 365+/-3 nm.
Design, chemical synthesis, and expression of genes for the three human color vision pigments.
The spectra are the first to be obtained from isolated human color vision pigments and confirm the original identification of the three color vision genes, which was based on genetic evidence.
Properties and Photoactivity of Rhodopsin Mutants
- Biology, Chemistry
Systematic analysis of the chromophore-binding pocket in rhodopsin and cone pigments has led to an improved understanding of the mechanism of the opsin-shift, and of particular molecular determinants underlying color vision in humans.
The molecular genetics of red and green color vision in mammals.
The additive effects of these amino acid changes fully explain the red-green color vision in a wide range of mammalian species, goldfish, American chameleon (Anolis carolinensis), and pigeon (Columba livia).
Cloning and expression of a Xenopus short wavelength cone pigment.
- BiologyExperimental eye research
The short wavelength visual pigment from Xenopus responsible for vision in the blue/violet portion of the spectrum was characterized by sequence spectroscopic analysis and permitted for the first time determination of the extinction coefficient, reactivity to hydroxylamine and presence of a Schiff base.