Rhodopsins from three frog and toad species: Sequences and functional comparisons

Experimental Eye Research

Volumn 66, Issue 3, 1998, Pages 295-305

  Fyhrquist, Nanna ^a   Donner, Kristian ^a   Hargrave, Paul A ^b   McDowell, J Hugh ^b   Popp, Michael P ^b   Smith, W Clay ^b  

^a UNIVERSITY OF HELSINKI   (Finland)

^b UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

Author keywords

Amino acid sequence; Frog rhodopsin; Spectral sensitivity; Thermal stability; Visual pigment

Indexed keywords

COMPLEMENTARY DNA; HYDROXYL GROUP; MESSENGER RNA; PHENYLALANINE; RHODOPSIN; SERINE; THREONINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DNA SEQUENCE; FROG; NONHUMAN; NUCLEOTIDE SEQUENCE; PIGMENT EPITHELIUM; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN STABILITY; RETINA ROD; THERMOSTABILITY; TOAD; XENOPUS LAEVIS;

EID: 0032033777     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1997.0430     Document Type: Article

References (54)

1. Autrum H. Uber kleinste Reize bei Sinnesorganen. Biol. Zentralbl. 63:1943;209-236.
2. Baldwin J. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12:1993;1693-1703.
3. Barlow H. B. Retinal noise and absolute threshold. Opt. Soc. Am. 46:1956;634-639.
4. Barlow H. B. Purkinje shift and retinal noise. Nature. 179:1957;255-256.
5. Barlow R. B., Birge R. R., Kaplan E., Tallent J. R. On the molecular origin of photoreceptor noise. Nature. 366:1993;64-66.
6. Batni S., Scalzetti L., Moody S. A., Knox B. E. Characterization of theXenopus. J. Biol. Chem. 271:1996;3179-3186.
7. Baylor D. A., Lamb T. D., Yau K.-W. Responses of retinal rods to single photons. J. Physiol. 288:1979;613-634.
8. Baylor D. A., Matthews G., Yau K.-W. Two components of electrical dark noise in toad retinal rod outer segments. J. Physiol. 309:1980;591-621.
9. Baylor, D. A., Nunn, B. J. and Schnapf, J. L. (1984). The photocurrent, noise and spectral sensitivity of rods of the monkey Macaca fascicularis. J. Physiol. 357, 575-607.
10. Blair W. F. Amphibians, their evolutionary history, taxonomy, and ecological adaptations. The amphibian visual system. 1976;Academic Press Inc. p. 1-27.
11. Bownds D. Site of attachment of retinal in rhodopsin. Nature. 216:1967;1178-1181.
12. Cantor C. R., Schimmel P. R. Biophysical chemistry. 1980;Freeman & Company.
13. Chen N., Ma J.-x., Corson D. W., Hazard E. S., Crouch R. K. Molecular cloning of a rhodopsin gene from salamander rods. Invest. Ophthalmol. Vis. Sci. 37:1996;1907-1913.
14. Corson D. W., Cornwall M. C., MacNichol E. F., Venkatchalam M., Crouch R. K. Transduction noise induced by 4-hydroxy retinals in rod photoreceptors. Biophys. J. 57:1990;109-115.
15. Crescitelli F. The visual pigment system ofXenopus laevis. Vis. Res. 13:1973;855-865.
16. Dartnall H. J. A. The visual pigment of the green rods. Vis. Res. 7:1967;1-6.
17. Dartnall H. J. A., Lythgoe J. N. The spectral clustering of visual pigments. Vis. Res. 5:1965;81-100.
18. de Vries H. Der Einfluss der Temperatur des Auges auf die spektrale Empfindlichkeitskurve. Experientia. 4:1948;357-358.
19. Donner K., Firsov M. L., Govardovskii V. I. The frequency of isomerization-like 'dark' events in rhodopsin and porphyropsin rods of the bullfrog retina. J. Physiol. 428:1990;673-692.
20. Firsov, M. L. and Govardovskii, V. I. (1990). Dark noise of visual pigments with different absorption maxima. Sensornye Sistemy 4, 25-34, (in Russian).
21. Fyhrquist, N. F., Govardovskii, V. I., Leibrock, C. and Reuter, T. (1998). Rod pigment and rod noise in the european toad Bufo bufo. Vis. Res. 38, 483-86.
22. Hargrave P. A., McDowell J. H., Curtis D. R., Wang J. K., Juszczak E., Fong S.-L., Rao J. K. M., Argos P. The structure of bovine rhodopsin. Biophys. Struct. Mech. 9:1983;235-244.
23. Hárosi F. I. Absorption spectra and linear dichroism of some amphibian photoreceptors. J. Gen. Physiol. 66:1975;357-382.
24. Hunt D. M., Fitzgibbon J., Slobodyanyuk S. J., Bowmaker J. K. Spectral tuning and molecular evolution of rod visual pigments in the species flock of cottoid fish in Lake Baikal. Vis. Res. 36:1996;1217-1224.
25. Karnik S. S., Sakmar T. P., Chen H.-B., Khorana H. G. Cysteine residues 110 and 187 are essential for the formation of the correct structure in bovine rhodopsin. Proc. Natl. Acad. Sci. U.S.A. 85:1988;8459-8463.
26. Kayada, S., Hisatomi, O. and Tokunaga, F. (1995). Cloning and expression of frog rhodopsin cDNA. Comp. Biochem. Physiol. 110B, 599-604.
27. Khorana H. G. Rhodopsin, photoreceptor of the rod cell. J. Biol. Chem. 267:1992;1-4.
28. Koskelainen A., Hemilä S., Donner K. Spectral sensitivities of short- and long-wavelength sensitive cone mechanisms in the frog retina. Acta Physiol. Scand. 152:1994;115-124.
29. Liebman, P. A. and Entine, G. (1968). Visual pigments of frog and tadpole (Rana pipiens). Vis. Res. 8, 761-75.
30. Makino-Tasaka, M. and Suzuki, T. (1984). The green rod pigment of the bullfrog, Rana catesbeiana. Vis. Res. 24, 309-22.
31. Matthews G. Dark noise in the outer segment membrane current of green rod photoreceptors from toad retina. J. Physiol. 349:1984;607-618.
32. Morris A., Bowmaker J. K., Hunt D. M. The molecular basis of a spectral shift in the rhodopsins of two species of squid from different photic environments. Proc. R. Soc. Lond. B. 254:1993;233-240.
33. Nakayama T. A., Khorana H. G. Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin. J. Biol. Chem. 266:1991;4269-4275.
34. Nathans J. Determinants of visual pigment absorbance: role of charged amino acids in the putative transmembrane segments. Biochemistry. 29:1990;937-942.
35. Nathans J. Rhodopsin: structure, function and genetics. Biochemistry. 31:1992;4923-4931.
36. Neitz M., Neitz J., Jacobs G. H. Spectral tuning underlying red-green color vision. Science. 252:1991;917-974.
37. Peskin J. C. The visual pigments of amphibians. Anat. Rec. 128:1957;600.
38. Pittler J. P., Fliesler S. T., Baehr W. Primary structure of frog rhodopsin. FEBS Lett. 313:1993;103-108.
39. Pugh E. N. Jr., Lamb T. D. Cyclic GMP and calcium: the internal messengers of excitation and adaptation in vertebrate photoreceptors. Vis. Res. 30:1990;1923-1948.
40. Reuter T. Visual pigments and ganglion cell activity in the retinae of tadpoles and adult frogs (Rana temporaria L. Acta Zool. Fenn. 122:1969;1-64.
41. Reuter T., Virtanen K. Color discrimination mechanisms in the retina of the toad (Bufo bufo. J. Comp. Physiol. 109:1976;337-343.
42. Reuter T. E., White R. H., Wald G. Rhodopsin and porphyropsin fields in the adult bullfrog retina. J. Gen. Physiol. 58:1971;351-371.
43. Sakmar T. P., Franke R. R., Khorana H. G. Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc. Natl. Acad. Sci. U.S.A. 86:1989;8309-8313.
44. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-termination inhibitors. Proc. Natl. Acad. Sci. U.S.A. 74:1977;5463-5467.
45. Savage J. M. The geographic distribution of frogs: patterns and predictions. Vial J. L. Evolutionary biology of anurans. 1973;351-445 University of Missouri Press.
46. Smith W. C., Adamus G., van der Wel H., Timmers A., Palczewski K., Ulshafer R. J., Hargrave P. A., McDowell J. H. Alligator rhodopsin: sequence and biochemical properties. Exp. Eye Res. 61:1995;569-578.
47. Stiles W. S. The physical interpretation of the spectral sensitivity curve of the eye. Transactions of the optical convention of the Worshipful Company of Spectacle Makers. 1948;Spectacle Makers' Co. p. 97-107.
48. Swofford D. L. PAUP: Phylogenetic analysis using parsimony, version 3.1. 1993.
49. Thompson J. D., Higgins D. G., Gibson T. J. Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
50. Wald G. The chemical evolution of vision. Harvey Lect. 41:1947;117-160.
51. Wang J. K., McDowell J. H., Hargrave P. A. Site of attachment of 11-cis. Biochemistry. 19:1980;5111-5117.
52. Weitz C. J., Nathans J. Histidine residues regulate the transition of photoexcited rhodopsin to its active conformation, metarhodopsin II. Neuron. 8:1992;465-472.
53. Yokoyama R., Knox B. E., Yokoyama S. Rhodopsin from the fish,Astyanax: Invest. Ophthalmol. Vis. Sci. 36:1995;939-945.
54. Zhukovsky E. A., Oprian D. D. Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science. 246:1989;928-930.