Primary structure of a visual pigment in bullfrog green rods

Hisatomi, Osamu; Takahashi, Yusuke; Taniguchi, Yoshihiro; Tsukahara, Yasuo; Tokunaga, Fumio

doi:10.1016/s0014-5793(99)00209-4

Cited by 41 publications

(45 citation statements)

References 34 publications

(46 reference statements)

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“…Primer sequences are as follows: 5′-ATGAGCAAAGGTCGACCAGA-3′ (forward) and 5′-TTATGCAGGAGTCACC-TGGCTGC-3′ (reverse). American bullfrog (L. catesbeianus) blue-sensitive cone pigment (AB010085) and Japanese fire-bellied newt (C. pyrrhogaster) blue-sensitive cone pigment (AB040148) were isolated as described previously (12,13). The cDNAs containing a point mutation were constructed using an In-Fusion cloning kit (Clontech) according to the manufacturer's instructions.…”

Section: Methodsmentioning

confidence: 99%

“…Moreover, amphibian species belonging to Anura and several genera in Urodela, including Hynobius and Ambystoma, but neither Cynops nor Salamandra, are unique in possessing two types of rods, red and green rods. Red rods are the normal rods that express rhodopsin, whereas green rods express a bluesensitive cone pigment (12)(13)(14)(15)(16). Thus, our goal was to determine whether the blue-sensitive cone pigments in green rods exhibit molecular properties similar to that of rhodopsin or to that of a typical cone pigment in cones.…”

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confidence: 99%

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Adaptation of cone pigments found in green rods for scotopic vision through a single amino acid mutation

Kojima

Matsutani

Yamashita

et al. 2017

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

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Most vertebrate retinas contain a single type of rod for scotopic vision and multiple types of cones for photopic and color vision. The retinas of certain amphibian species uniquely contain two types of rods: red rods, which express rhodopsin, and green rods, which express a blue-sensitive cone pigment (M1/SWS2 group). Spontaneous activation of rhodopsin induced by thermal isomerization of the retinal chromophore has been suggested to contribute to the rod's background noise, which limits the visual threshold for scotopic vision. Therefore, rhodopsin must exhibit low thermal isomerization rate compared with cone visual pigments to adapt to scotopic condition. In this study, we determined whether amphibian blue-sensitive cone pigments in green rods exhibit low thermal isomerization rates to act as rhodopsin-like pigments for scotopic vision. Anura blue-sensitive cone pigments exhibit low thermal isomerization rates similar to rhodopsin, whereas Urodela pigments exhibit high rates like other vertebrate cone pigments present in cones. Furthermore, by mutational analysis, we identified a key amino acid residue, Thr47, that is responsible for the low thermal isomerization rates of Anura blue-sensitive cone pigments. These results strongly suggest that, through this mutation, anurans acquired special blue-sensitive cone pigments in their green rods, which could form the molecular basis for scotopic color vision with normal red rods containing green-sensitive rhodopsin.photoreceptor cell | visual pigment | amphibian | molecular evolution | color discrimination

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Adaptation of cone pigments found in green rods for scotopic vision through a single amino acid mutation

Kojima

Matsutani

Yamashita

et al. 2017

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

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“…Immunophenotypic analysis was carried out in frozen sections for the proliferating cell analysis and undifferentiated and differentiated P1-P3 cells for lineage analysis, using primary antibodies against Ki-67 (antigen retrieval, 1:50, mouse, Zymed, South San Francisco, CA), BrdU (1:400, sheep, Biodesign International, Saco, ME), nestin (Rat-401, 1:50, mouse, DSHB, Iowa City, IA), neuron-specific enolase (NSE, 1:10,000, rabbit, DAKO, Burlingame, CA), ␤III tubulin (1:200, mouse, ICN Pharmaceuticals, Costa Mesa, CA), synaptophysin (1:500, mouse, Sigma Chemical), rhodopsin [rho 1D4, 1:50, mouse, gift from Robert S. Molday (14)], S-antigen [arrestin, A9C6, 1:10,000, mouse, gift from Larry A. Donoso (9)], recoverin [1:200, rabbit, gift from T. Mü ller (15)], protein kinase C (␣ isoform, 1:50, mouse, Amersham Pharmacia Biotech, Piscataway, NJ), calbindin (1:1,000, rabbit, Calbiochem, San Diego, CA), calretinin (1:500, rabbit, Chemicon, Temecula, CA), glial fibrillary acidic protein (GFAP, 1:10,000, mouse, Sigma Chemical), and galactocerebroside (GalC, 1:50, rabbit, Advanced Immunochemical, Long Beach, CA). Briefly, the cultured cells and tissue sections were incubated in 20% goat normal serum in PBS containing 0.25% Triton X-100 (PBST) for 30 min at room temperature followed by incubation with primary antibodies for 20 h at 4°C.…”

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In Vitro Isolation and Expansion of Human Retinal Progenitor Cells

Yang

2002

Experimental Neurology

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Human retinal development proceeds with temporal and spatial precision. Although differentiation starts around the beginning of the third month of gestation, the majority of cells in the outer neuroblastic layer of human neural retina are still proliferating, as evidenced by their Ki-67 immunoreactivity. In the present study, the proliferating human retinal progenitor cells (HRPCs) were isolated and expanded in culture. They were capable of dividing for multiple generations (with passage 8, the latest tested) and differentiating to several retinal cell phenotypes. These findings indicate that human retina at the 10th-13th week of gestation harbors progenitor cells that can be maintained and expanded in vitro for multiple generations. The availability of such cells may have important implications with respect to human degenerative retinal diseases, as these HRPCs have the potential to be used therapeutically to replace damaged retinal neurons. © 2002 Elsevier Science (USA)

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“…Additionally, the following SWS2 opsins of non-fish vertebrates were used as outgroups: newt (Cynops pyrrhogaster) (GenBank TM accession number AB040148) (13), salamander (Ambystoma tigrinum) (GenBank TM accession number AF038946) (18), bull frog (Rana catesbeiana) (GenBank TM accession number AB010085) (19), American chameleon (Anolis carolinensis) (GenBank TM accession number AF133907) (20,21), zebrafinch (Taeniopygia guttata) (GenBank TM accession number AF222332) (22), chicken (Gallus gallus) (GenBank TM accession number P28682) (23,24), and pigeon (Columba livia) (GenBank TM accession number Af149238) (25).…”

Section: Methodsmentioning

confidence: 99%

Spectral Differentiation of Blue Opsins between Phylogenetically Close but Ecologically Distant Goldfish and Zebrafish

Chinen

Matsumoto

Kawamura

2005

Journal of Biological Chemistry

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Zebrafish and goldfish are both diurnal freshwater fish species belonging to the same family, Cyprinidae, but their visual ecological surroundings considerably differ. Zebrafish are surface swimmers in conditions of broad and shortwave-dominated background spectra and goldfish are generalized swimmers whose light environment extends to a depth of elevated short wavelength absorbance with turbidity. The peak absorption spectrum ( max ) of the zebrafish blue (SWS2) visual pigment is consistently shifted to short wavelength (416 nm) compared with that of the goldfish SWS2 (443 nm). Among the amino acid differences between the two pigments, only one (alanine in zebrafish and serine in goldfish at residue 94) was previously known to cause a difference in absorption spectrum (14-nm max shift in newt SWS2). In this study, we reconstructed the ancestral SWS2 pigment of the two species by applying likelihood-based Bayesian statistics and performing sitedirected mutagenesis. The reconstituted ancestral photopigment had a max of 430 nm, indicating that zebrafish and goldfish achieved short wavelength (؊14 nm) and long wavelength (؉13 nm) spectral shifts, respectively, from the ancestor. Unexpectedly, the S94A mutation resulted in only a ؊3-nm spectral shift when introduced into the goldfish SWS2 pigment. Nearly half of the long wavelength shift toward the goldfish pigment was achieved instead by T116L (6 nm). The S295C mutation toward zebrafish SWS2 contributed to creating a ridge of absorbance around 400 nm and broadening its spectral sensitivity in the short wavelength direction. These results indicate that the evolutionary engineering approach is very effective in deciphering the process of functional divergence of visual pigments.Vertebrate visual pigments consist of a protein moiety (i.e. opsin), and a chromophore, either 11-cis-retinal (vitamin A1 aldehyde) or 11-cis 3,4-dehydroretinal (vitamin A2 aldehyde). These pigments reside in rod and cone photoreceptor cells in the retina. Rods are used for dim light vision, and cones are used for daylight and color vision. Vertebrate visual opsins can be classified into five phylogenetic groups: RH1 1 (rod opsin or rhodopsin), RH2 (RH1-like, or green, cone opsin), SWS1 (short wavelength-sensitive type 1, or UV-blue, cone opsin), SWS2 (short wavelength-sensitive type 2, or blue, cone opsin), and M/LWS (middle to long wavelength-sensitive, or red-green, cone opsin) (1). When an opsin forms a photopigment with the A2 chromophore, its peak absorption spectrum ( max ) is located at a longer wavelength than it forms with the A1 chromophore. The spectral shift is wavelength-dependent; it can be as great as 60 nm at longer wavelengths, and as little as 5-10 nm at shorter wavelengths (2, 3).Despite having all five types of opsins in common and sharing ancestry in the same family Cyprinidae, zebrafish (Danio rerio) and goldfish (Carassius auratus) use different chromophores, A1 and A2, respectively, under normal conditions (4 -6). This is consistent with the differences in their visual...

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Primary structure of a visual pigment in bullfrog green rods

Cited by 41 publications

References 34 publications

Adaptation of cone pigments found in green rods for scotopic vision through a single amino acid mutation

Adaptation of cone pigments found in green rods for scotopic vision through a single amino acid mutation

In Vitro Isolation and Expansion of Human Retinal Progenitor Cells

Spectral Differentiation of Blue Opsins between Phylogenetically Close but Ecologically Distant Goldfish and Zebrafish

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