scholarly journals Genetic Analyses of Visual Pigments of the Pigeon (Columba livia)

Genetics ◽  
1999 ◽  
Vol 153 (4) ◽  
pp. 1839-1850 ◽  
Author(s):  
Shoji Kawamura ◽  
Nathan S Blow ◽  
Shozo Yokoyama
Keyword(s):  
Pineal Gland ◽  
Columba Livia ◽  
Visual Pigments ◽  
Genetic Analyses ◽  
Opsin Genes ◽  
Uv Vision ◽  
Absorbance Spectra

AbstractWe isolated five classes of retinal opsin genes rh1Cl, rh2Cl, sws1Cl, sws2Cl, and lwsCl from the pigeon; these encode RH1Cl, RH2Cl, SWS1Cl, SWS2Cl, and LWSCl opsins, respectively. Upon binding to 11-cis-retinal, these opsins regenerate the corresponding photosensitive molecules, visual pigments. The absorbance spectra of visual pigments have a broad bell shape with the peak, being called λmax. Previously, the SWS1Cl opsin cDNA was isolated from the pigeon retinal RNA, expressed in cultured COS1 cells, reconstituted with 11-cis-retinal, and the λmax of the resulting SWS1Cl pigment was shown to be 393 nm. In this article, using the same methods, the λmax values of RH1Cl, RH2Cl, SWS2Cl, and LWSCl pigments were determined to be 502, 503, 448, and 559 nm, respectively. The pigeon is also known for its UV vision, detecting light at 320–380 nm. Being the only pigments that absorb light below 400 nm, the SWS1Cl pigments must mediate its UV vision. We also determined that a nonretinal PCl pigment in the pineal gland of the pigeon has a λmax value at 481 nm.

Deep-sea and pelagic rod visual pigments identified in the mysticete whales

2012 ◽  
Vol 29 (2) ◽  
pp. 95-103 ◽  
Author(s):  
NICOLE BISCHOFF ◽  
BENJAMIN NICKLE ◽  
THOMAS W. CRONIN ◽  
STEPHANI VELASQUEZ ◽  
JEFFRY I. FASICK
Keyword(s):  
Amino Acid ◽  
Deep Sea ◽  
Foraging Strategy ◽  
Visual Pigments ◽  
Amino Acid Substitutions ◽  
Gray Whale ◽  
Difference Spectra ◽  
Terrestrial Mammals ◽  
Opsin Genes ◽  
Absorbance Spectra

AbstractOur current understanding of the spectral sensitivities of the mysticete whale rod-based visual pigments is based on two species, the gray whale (Eschrichtius robustus) and the humpback whale (Megaptera novaeangliae) possessing absorbance maxima determined from difference spectra to be 492 and 497 nm, respectively. These absorbance maxima values are blueshifted relative to those from typical terrestrial mammals (≈500 nm) but are redshifted when compared to those identified in the odontocetes (479–484 nm). Although these mysticete species represent two of the four mysticete families, they do not fully represent the mysticete whales in terms of foraging strategy and underwater photic environments where foraging occurs. In order to better understand the spectral sensitivities of the mysticete whale rod visual pigments, we have examined the rod opsin genes from 11 mysticete species and their associated amino acid substitutions. Based on the amino acids occurring at positions 83, 292, and 299 along with the directly determined dark spectra from expressed odontocete and mysticete rod visual pigments, we have determined that the majority of mysticete whales possess deep-sea and pelagic like rod visual pigments with absorbance maxima between 479 and 484 nm. Finally, we have defined the five amino acid substitution events that determine the resulting absorbance spectra and associated absorbance maxima for the mysticete whale rod visual pigments examined here.

scholarly journals Euphausiid visual pigments. The rhodopsins of Euphausia superba and Meganyctiphanes norvegica (Crustacea, Euphausiacea).

1982 ◽  
Vol 80 (3) ◽  
pp. 451-472 ◽  
Author(s):  
C J Denys ◽  
P K Brown
Keyword(s):  
Schiff Base ◽  
Euphausia Superba ◽  
Visual Pigments ◽  
Long Wavelength ◽  
Spectral Changes ◽  
Accessory Pigment ◽  
Meganyctiphanes Norvegica ◽  
Ph Dependent ◽  
Wavelength Light ◽  
Absorbance Spectra

The rhabdoms of Euphausia superba contain one digitonin-extractable rhodopsin, lambda max 485 nm. The rhodopsin undergoes unusual pH-dependent spectral changes: above neutrality, the absorbance decreases progressively at 485 nm and rises near 370 nm. This change is reversible and appears to reflect an equilibrium between a protonated and an unprotonated form of the rhodopsin Schiff-base linkage. Near neutral pH and at 10 degrees C, the rhodopsin is partiaLly converted by 420-nm light to a stable 493-nm metarhodopsin. The metarhodopsin is partially photoconverted to rhodopsin by long-wavelength light in the absence of NH2OH; in the presence of NH2OH, it is slowly converted to retinal oxime and opsin. The rhodopsin of Meganyctiphanes norvegica measured in fresh rhabdoms by microspectrophotometry has properties very similar to those of the extracted rhodopsin of E. superba. Its lambda max is 488 nm and it is partially photoconverted by short wavelength irradiation to a stable photoconvertible metarhodopsin similar to that of E. superba. In the presence of light and NH2OH, the M. norvegica metarhodopsin is converted to retinal oxime and opsin. Our results indicate that previous determinations of euphausiid rhodopsin absorbance spectra were incorrect because of accessory pigment contamination.

Visual pigments in the sea lamprey, Petromyzon marinus

1993 ◽  
Vol 10 (4) ◽  
pp. 711-715 ◽  
Author(s):  
Ferenc I. Hárosi ◽  
Jochen Kleinschmidt
Keyword(s):  
Common Ancestor ◽  
Petromyzon Marinus ◽  
Sea Lamprey ◽  
Visual Pigments ◽  
Maximum Value ◽  
Opsin Genes

AbstractWe present microspectrophotometric evidence for the existence of two distinct visual pigments residing in two different morphological types of photoreceptor of the sea lamprey. In the upstream migrant Petromyzon marinus, the pigment found in short receptors has a wavelength of peak absorbance (λmax) of 525 nm, whereas the pigment located in long receptors has a λmax of 600 nm. Although the former appears to be pure porphyropsin, the latter is akin to visual pigments found in the red-absorbing cones of amphibian and teleost retinae. The kinship is more than superficial pertaining to λmax of the a–band absorbance to its native maximum value. The presence of an anion-sensitive and an anion-insensitive pigment in a retina implies the expression of two distinct opsin genes. We infer this from several examples of correlation between anion sensitivity and opsin sequence groupings. Moreover, the presence of two distinct opsin genes expressed throughout six vertebrate classes implies their existence in a common ancestor to all.

Photoreceptors and visual pigments in the red-eared turtle, Trachemys scripta elegans

2001 ◽  
Vol 18 (5) ◽  
pp. 753-757 ◽  
Author(s):  
E.R. LOEW ◽  
V.I. GOVARDOVSKII
Keyword(s):  
Visual Pigments ◽  
Trachemys Scripta ◽  
Trachemys Scripta Elegans ◽  
Oil Droplets ◽  
Orange Oil ◽  
Oil Droplet ◽  
Cone System ◽  
Complex Cone ◽  
The Moment ◽  
Absorbance Spectra

Absorbance spectra of cone outer segments and oil droplets were recorded microspectrophotometrically in the retina of the red-eared turtle, Trachemys scripta elegans. There are four cone visual pigments, with λmax = 617 nm (red sensitive), 515 nm (green sensitive), 458 nm (blue sensitive), and 372 nm (UV-sensitive). The red-sensitive pigment resides in single cones with red or orange oil droplets, and in both members of double cones. The principal member of the double cone contains an orange oil droplet, and the accessory member is droplet free. The green-sensitive pigment is situated in single cones with orange/dark yellow droplets. The blue-sensitive pigment is combined with the UV-absorbing oil droplet in single cones. The UV-sensitive pigment resides in single cones with clear oil droplets that exhibited virtually no absorbance down to 325 nm. Thus, seven types of cones can be identified based on their morphology, oil droplet color, and the visual pigment absorbance. At the moment, this is the most complex cone system described for vertebrates.

scholarly journals In search of the visual pigment template

2000 ◽  
Vol 17 (4) ◽  
pp. 509-528 ◽  
Author(s):  
VICTOR I. GOVARDOVSKII ◽  
NANNA FYHRQUIST ◽  
TOM REUTER ◽  
DMITRY G. KUZMIN ◽  
KRISTIAN DONNER
Keyword(s):  
Visual Pigment ◽  
Good Description ◽  
Visual Pigments ◽  
Rod Outer Segments ◽  
Absorbance Spectrum ◽  
Outer Segments ◽  
Bovine Rhodopsin ◽  
Α Band ◽  
Absorbance Spectra

Absorbance spectra were recorded by microspectrophotometry from 39 different rod and cone types representing amphibians, reptiles, and fishes, with A1- or A2-based visual pigments and λmax ranging from 357 to 620 nm. The purpose was to investigate accuracy limits of putative universal templates for visual pigment absorbance spectra, and if possible to amend the templates to overcome the limitations. It was found that (1) the absorbance spectrum of frog rhodopsin extract very precisely parallels that of rod outer segments from the same individual, with only a slight hypsochromic shift in λmax, hence templates based on extracts are valid for absorbance in situ; (2) a template based on the bovine rhodopsin extract data of Partridge and De Grip (1991) describes the absorbance of amphibian rod outer segments excellently, contrary to recent electrophysiological results; (3) the λmax/λ invariance of spectral shape fails for A1 pigments with small λmax and for A2 pigments with large λmax, but the deviations are systematic and can be readily incorporated into, for example, the Lamb (1995) template. We thus propose modified templates for the main “α-band” of A1 and A2 pigments and show that these describe both absorbance and spectral sensitivities of photoreceptors over the whole range of λmax. Subtraction of the α-band from the full absorbance spectrum leaves a “β-band” described by a λmax-dependent Gaussian. We conclude that the idea of universal templates (one for A1- and one for A2-based visual pigments) remains valid and useful at the present level of accuracy of data on photoreceptor absorbance and sensitivity. The sum of our expressions for the α- and β-band gives a good description for visual pigment spectra with λmax > 350 nm.

scholarly journals Why UV vision and red vision are important for damselfish (Pomacentridae): structural and expression variation in opsin genes

2017 ◽  
Vol 26 (5) ◽  
pp. 1323-1342 ◽  
Author(s):  
Sara M. Stieb ◽  
Fabio Cortesi ◽  
Lorenz Sueess ◽  
Karen L. Carleton ◽  
Walter Salzburger ◽  
...  
Keyword(s):  
Expression Variation ◽  
Opsin Genes ◽  
Uv Vision

Molecular diversity of visual pigments in Stomatopoda (Crustacea)

2009 ◽  
Vol 26 (3) ◽  
pp. 255-265 ◽  
Author(s):  
MEGAN L. PORTER ◽  
MICHAEL J. BOK ◽  
PHYLLIS R. ROBINSON ◽  
THOMAS W. CRONIN
Keyword(s):  
Gene Duplication ◽  
Molecular Diversity ◽  
Visual Complexity ◽  
Binding Pocket ◽  
Acid Sites ◽  
Visual Pigments ◽  
Long Wavelength ◽  
Anatomy And Physiology ◽  
Opsin Genes ◽  
Duplication Events

AbstractStomatopod crustaceans possess apposition compound eyes that contain more photoreceptor types than any other animal described. While the anatomy and physiology of this complexity have been studied for more than two decades, few studies have investigated the molecular aspects underlying the stomatopod visual complexity. Based on previous studies of the structure and function of the different types of photoreceptors, stomatopod retinas are hypothesized to contain up to 16 different visual pigments, with 6 of these having sensitivity to middle or long wavelengths of light. We investigated stomatopod middle- and long-wavelength-sensitive opsin genes from five species with the hypothesis that each species investigated would express up to six different opsin genes. In order to understand the evolution of this class of stomatopod opsins, we examined the complement of expressed transcripts in the retinas of species representing a broad taxonomic range (four families and three superfamilies). A total of 54 unique retinal opsins were isolated, resulting in 6–15 different expressed transcripts in each species. Phylogenetically, these transcripts form six distinct clades, grouping with other crustacean opsins and sister to insect long-wavelength visual pigments. Within these stomatopod opsin groups, intra- and interspecific clusters of highly similar transcripts suggest that there has been rampant recent gene duplication. Some of the observed molecular diversity is also due to ancient gene duplication events within the stem crustacean lineage. Using evolutionary trace analysis, 10 amino acid sites were identified as functionally divergent among the six stomatopod opsin clades. These sites form tight clusters in two regions of the opsin protein known to be functionally important: six in the chromophore-binding pocket and four at the cytoplasmic surface in loops II and III. These two clusters of sites indicate that stomatopod opsins have diverged with respect to both spectral tuning and signal transduction.

scholarly journals Spectral tuning by opsin coexpression in retinal regions that view different parts of the visual field

2014 ◽  
Vol 281 (1797) ◽  
pp. 20141980 ◽  
Author(s):  
Brian E. Dalton ◽  
Ellis R. Loew ◽  
Thomas W. Cronin ◽  
Karen L. Carleton
Keyword(s):  
Visual Field ◽  
Visual Pigment ◽  
Cichlid Fish ◽  
Visual Pigments ◽  
Colour Discrimination ◽  
Spectral Tuning ◽  
Trade Off ◽  
Opsin Genes ◽  
First Time ◽  
Different Parts

Vision frequently mediates critical behaviours, and photoreceptors must respond to the light available to accomplish these tasks. Most photoreceptors are thought to contain a single visual pigment, an opsin protein bound to a chromophore, which together determine spectral sensitivity. Mechanisms of spectral tuning include altering the opsin, changing the chromophore and incorporating pre-receptor filtering. A few exceptions to the use of a single visual pigment have been documented in which a single mature photoreceptor coexpresses opsins that form spectrally distinct visual pigments, and in these exceptions the functional significance of coexpression is unclear. Here we document for the first time photoreceptors coexpressing spectrally distinct opsin genes in a manner that tunes sensitivity to the light environment. Photoreceptors of the cichlid fish, Metriaclima zebra , mix different pairs of opsins in retinal regions that view distinct backgrounds. The mixing of visual pigments increases absorbance of the corresponding background, potentially aiding the detection of dark objects. Thus, opsin coexpression may be a novel mechanism of spectral tuning that could be useful for detecting prey, predators and mates. However, our calculations show that coexpression of some opsins can hinder colour discrimination, creating a trade-off between visual functions.

Sign in / Sign up

Export Citation Format

Share Document