Efficiencies of activation of transducin by cone and rod visual pigments

Biochemistry

Volumn 52, Issue 17, 2013, Pages 3010-3018

  Imamoto, Yasushi ^a   Seki, Ichirota ^a   Yamashita, Takahiro ^a   Shichida, Yoshinori ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION EFFICIENCY; ACTIVATION PROCESS; AMINO ACID RESIDUES; BIOCHEMICAL METHODS; INITIAL VELOCITIES; INTRINSIC FLUORESCENCE; MICHAELIS CONSTANTS; TRYPTOPHAN RESIDUES;

ACTIVATION ANALYSIS; AMINO ACIDS; CHROMOPHORES; EFFICIENCY; FUNCTIONAL GROUPS; HYDROLYSIS; VISION;

CHEMICAL ACTIVATION;

RHODOPSIN; TRANSDUCIN; TRYPTOPHAN; VISUAL PIGMENT;

ARTICLE; CHICKEN; CHROMATOPHORE; COW; ENZYME ACTIVATION; ENZYME CONFORMATION; HYDROLYSIS; MICHAELIS CONSTANT; NONHUMAN; PHOTORECEPTOR; PRIORITY JOURNAL;

ANIMALS; CHICKENS; FLUORESCENCE; HYDROLYSIS; RETINAL CONE PHOTORECEPTOR CELLS; RETINAL PIGMENTS; RETINAL ROD PHOTORECEPTOR CELLS; TRANSDUCIN;

BOVINAE;

EID: 84877028283     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3015967     Document Type: Article

References (42)

1. Shichida, Y. and Matsuyama, T. (2009) Evolution of opsins and phototransduction Philos. Trans. R. Soc., B 364, 2881-2895
2. Shichida, Y., Imai, H., Imamoto, Y., Fukada, Y., and Yoshizawa, T. (1994) Is chicken green-sensitive cone visual pigment a rhodopsin-like pigment? A comparative study of the molecular properties between chicken green and rhodopsin Biochemistry 33, 9040-9044
3. Okada, T., Matsuda, T., Kandori, H., Fukada, Y., Yoshizawa, T., and Shichida, Y. (1994) Circular dichroism of metaiodopsin II and its binding to transducin: A comparative study between meta II intermediates of iodopsin and rhodopsin Biochemistry 33, 4940-4946
4. Imai, H., Imamoto, Y., Yoshizawa, T., and Shichida, Y. (1995) Difference in molecular properties between chicken green and rhodopsin as related to the functional difference between cone and rod photoreceptor cells Biochemistry 34, 10525-10531
5. Imai, H., Terakita, A., Tachibanaki, S., Imamoto, Y., Yoshizawa, T., and Shichida, Y. (1997) Photochemical and biochemical properties of chicken blue-sensitive cone visual pigment Biochemistry 36, 12773-12779
6. Tachibanaki, S., Tsushima, S., and Kawamura, S. (2001) Low amplification and fast visual pigment phosphorylation as mechanisms characterizing cone photoresponses Proc. Natl. Acad. Sci. U.S.A. 98, 14044-14049
7. Okano, T., Fukada, Y., Shichida, Y., and Yoshizawa, T. (1992) Photosensitivities of iodopsin and rhodopsins Photochem. Photobiol. 56, 995-1001
8. Kuwayama, S., Imai, H., Hirano, T., Terakita, A., and Shichida, Y. (2002) Conserved proline residue at position 189 in cone visual pigments as a determinant of molecular properties different from rhodopsins Biochemistry 41, 15245-15252
9. Imai, H., Kojima, D., Oura, T., Tachibanaki, S., Terakita, A., and Shichida, Y. (1997) Single amino acid residue as a functional determinant of rod and cone visual pigments Proc. Natl. Acad. Sci. U.S.A. 94, 2322-2326
10. Phillips, W. J. and Cerione, R. A. (1988) The intrinsic fluorescence of the α subunit of transducin. Measurement of receptor-dependent guanine nucleotide exchange J. Biol. Chem. 263, 15498-15505
11. Faurobert, E., Otto-Bruc, A., Chardin, P., and Chabre, M. (1993) Tryptophan W207 in transducin Tα is the fluorescence sensor of the G protein activation switch and is involved in the effector binding EMBO J. 12, 4191-4198
12. Ernst, O. P., Gramse, V., Kolbe, M., Hofmann, K. P., and Heck, M. (2007) Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit Proc. Natl. Acad. Sci. U.S.A. 104, 10859-10864
13. Farrens, D. L. and Khorana, H. G. (1995) Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy J. Biol. Chem. 270, 5073-5076
14. Hoersch, D., Otto, H., Wallat, I., and Heyn, M. P. (2008) Monitoring the conformational changes of photoactivated rhodopsin from microseconds to seconds by transient fluorescence spectroscopy Biochemistry 47, 11518-11527
15. Chen, M. H., Kuemmel, C., Birge, R. R., and Knox, B. E. (2012) Rapid release of retinal from a cone visual pigment following photoactivation Biochemistry 51, 4117-4125
16. Nathans, J. (1990) Determinants of visual pigment absorbance: Role of charged amino acids in the putative transmembrane segments Biochemistry 29, 937-942
17. Imai, H., Terakita, A., and Shichida, Y. (2000) Analysis of amino acid residues in rhodopsin and cone visual pigments that determine their molecular properties Methods Enzymol. 315, 293-312
18. Kuwayama, S., Imai, H., Morizumi, T., and Shichida, Y. (2005) Amino acid residues responsible for the meta-III decay rates in rod and cone visual pigments Biochemistry 44, 2208-2215
19. Tachibanaki, S., Imai, H., Mizukami, T., Okada, T., Imamoto, Y., Matsuda, T., Fukada, Y., Terakita, A., and Shichida, Y. (1997) Presence of two rhodopsin intermediates responsible for transducin activation Biochemistry 36, 14173-14180
20. Martin, E. L., Rens-Domiano, S., Schatz, P. J., and Hamm, H. E. (1996) Potent peptide analogues of a G protein receptor-binding region obtained with a combinatorial library J. Biol. Chem. 271, 361-366
21. Sakai, K., Imamoto, Y., Su, C. Y., Tsukamoto, H., Yamashita, T., Terakita, A., Yau, K. W., and Shichida, Y. (2012) Photochemical nature of parietopsin Biochemistry 51, 1933-1941
22. Imamoto, Y. and Shichida, Y. (2008) Thermal recovery of iodopsin from photobleaching intermediates Photochem. Photobiol. 84, 941-948
23. Sato, K., Yamashita, T., Imamoto, Y., and Shichida, Y. (2012) Comparative studies on the late bleaching processes of four kinds of cone visual pigments and rod visual pigment Biochemistry 51, 4300-4308
24. König, B., Welte, W., and Hofmann, K. P. (1989) Photoactivation of rhodopsin and interaction with transducin in detergent micelles. Effect of 'doping' with steroid molecules FEBS Lett. 257, 163-166
25. Imamoto, Y., Kataoka, M., Tokunaga, F., and Palczewski, K. (2000) Light-induced conformational changes of rhodopsin probed by fluorescent Alexa594 immobilized on the cytoplasmic surface Biochemistry 39, 15225-15233
26. Sato, K., Morizumi, T., Yamashita, T., and Shichida, Y. (2010) Direct observation of the pH-dependent equilibrium between metarhodopsins I and II and the pH-independent interaction of metarhodopsin II with transducin C-terminal peptide Biochemistry 49, 736-741
27. Deupi, X. and Standfuss, J. (2011) Structural insights into agonist-induced activation of G-protein-coupled receptors Curr. Opin. Struct. Biol. 21, 541-551
28. Jastrzebska, B., Palczewski, K., and Golczak, M. (2011) Role of bulk water in hydrolysis of the rhodopsin chromophore J. Biol. Chem. 286, 18930-18937
29. Heck, M., Schadel, S. A., Maretzki, D., Bartl, F. J., Ritter, E., Palczewski, K., and Hofmann, K. P. (2003) Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II J. Biol. Chem. 278, 3162-3169
30. Okano, T., Kojima, D., Fukada, Y., Shichida, Y., and Yoshizawa, T. (1992) Primary structures of chicken cone visual pigments: Vertebrate rhodopsins have evolved out of cone visual pigments Proc. Natl. Acad. Sci. U.S.A. 89, 5932-5936
31. Weitz, C. J. and Nathans, J. (1992) Histidine residues regulate the transition of photoexcited rhodopsin to its active conformation, metarhodopsin II Neuron 8, 465-472
32. Das, J., Crouch, R. K., Ma, J. X., Oprian, D. D., and Kono, M. (2004) Role of the 9-methyl group of retinal in cone visual pigments Biochemistry 43, 5532-5538
33. Estevez, M. E., Kolesnikov, A. V., Ala-Laurila, P., Crouch, R. K., Govardovskii, V. I., and Cornwall, M. C. (2009) The 9-methyl group of retinal is essential for rapid Meta II decay and phototransduction quenching in red cones J. Gen. Physiol. 134, 137-150
34. Choe, H. W., Kim, Y. J., Park, J. H., Morizumi, T., Pai, E. F., Krauss, N., Hofmann, K. P., Scheerer, P., and Ernst, O. P. (2011) Crystal structure of metarhodopsin II Nature 471, 651-655
35. Standfuss, J., Edwards, P. C., D'Antona, A., Fransen, M., Xie, G., Oprian, D. D., and Schertler, G. F. (2011) The structural basis of agonist-induced activation in constitutively active rhodopsin Nature 471, 656-660
36. Deng, W. T., Sakurai, K., Liu, J., Dinculescu, A., Li, J., Pang, J., Min, S. H., Chiodo, V. A., Boye, S. L., Chang, B., Kefalov, V. J., and Hauswirth, W. W. (2009) Functional interchangeability of rod and cone transducin α-subunit Proc. Natl. Acad. Sci. U.S.A. 106, 17681-17686
37. Gopalakrishna, K. N., Boyd, K. K., and Artemyev, N. O. (2012) Comparative analysis of cone and rod transducins using chimeric Gα subunit Biochemistry 51, 1617-1624
38. Bownds, D., Dawes, J., Miller, J., and Stahlman, M. (1972) Phosphorylation of frog photoreceptor membranes induced by light Nat. New Biol. 237, 125-127
39. Kühn, H., Cook, J. H., and Dreyer, W. J. (1973) Phosphorylation of rhodopsin in bovine photoreceptor membranes. A dark reaction after illumination Biochemistry 12, 2495-2502
40. Kennedy, M. J., Lee, K. A., Niemi, G. A., Craven, K. B., Garwin, G. G., Saari, J. C., and Hurley, J. B. (2001) Multiple phosphorylation of rhodopsin and the in vivo chemistry underlying rod photoreceptor dark adaptation Neuron 31, 87-101
41. Sakurai, K., Onishi, A., Imai, H., Chisaka, O., Ueda, Y., Usukura, J., Nakatani, K., and Shichida, Y. (2007) Physiological properties of rod photoreceptor cells in green-sensitive cone pigment knock-in mice J. Gen. Physiol. 130, 21-40
42. Shi, G., Yau, K. W., Chen, J., and Kefalov, V. J. (2007) Signaling properties of a short-wave cone visual pigment and its role in phototransduction J. Neurosci. 27, 10084-10093