메뉴 건너뛰기




Volumn 54, Issue 2-3, 2000, Pages 94-102

Key issues in the photochemistry and signalling-state formation of photosensor proteins

Author keywords

Chromophores; Context dependent conformational transition; Cryptochromes; Electron transfer; Isomerization; Photoactive yellow protein (PYP); Photolyase; Phytochromes; Rhodopsins; Xanthopsins

Indexed keywords

CHROMATOPHORE; ISOMERISM; MOLECULAR DYNAMICS; PHOTOCHEMISTRY; PHOTORECEPTOR; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ACTIVITY RELATION;

EID: 0034048749     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(00)00004-X     Document Type: Article
Times cited : (31)

References (63)
  • 2
    • 0032144042 scopus 로고    scopus 로고
    • The structure and mechanism of the family of retinal proteins from halophilic archaea
    • Oesterhelt D. The structure and mechanism of the family of retinal proteins from halophilic archaea. Curr. Opin. Struct. Biol. 8:1998;489-500.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 489-500
    • Oesterhelt, D.1
  • 3
    • 0032578425 scopus 로고    scopus 로고
    • The phytochrome family: Dissection of functional roles and signalling pathways among family members
    • Quail P.H. The phytochrome family: dissection of functional roles and signalling pathways among family members. Philos. Trans. R. Soc. Lond. B: Biol. Sci. 353:1998;1399-1403.
    • (1998) Philos. Trans. R. Soc. Lond. B: Biol. Sci. , vol.353 , pp. 1399-1403
    • Quail, P.H.1
  • 5
    • 0027493250 scopus 로고
    • HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor
    • Ahmad M., Cashmore A.R. HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor. Nature. 366:1993;162-166.
    • (1993) Nature , vol.366 , pp. 162-166
    • Ahmad, M.1    Cashmore, A.R.2
  • 7
    • 0029743968 scopus 로고    scopus 로고
    • Photobiology of microorganisms: How photosensors catch a photon to initialize signalling
    • Hellingwerf K.J., Hoff W.D., Crielaard W. Photobiology of microorganisms: how photosensors catch a photon to initialize signalling. Mol. Microbiol. 21:1996;683-693.
    • (1996) Mol. Microbiol. , vol.21 , pp. 683-693
    • Hellingwerf, K.J.1    Hoff, W.D.2    Crielaard, W.3
  • 9
    • 0032506138 scopus 로고    scopus 로고
    • Eukaryotic phytochromes: Light-regulated serine/threonine protein kinases with histidine kinase ancestry
    • Yeh K.C., Lagarias J.C. Eukaryotic phytochromes: light-regulated serine/threonine protein kinases with histidine kinase ancestry. Proc. Natl. Acad. Sci. USA. 95:1998;13976-13981.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13976-13981
    • Yeh, K.C.1    Lagarias, J.C.2
  • 10
    • 0032171109 scopus 로고    scopus 로고
    • Phytochrome-mediated light signals are transduced to nucleoside diphosphate kinase in Pisum sativum L. cv. Alaska
    • Tanaka N., Ogura T., Noguchi T., Hirano H., Yabe N., Hasunuma K. Phytochrome-mediated light signals are transduced to nucleoside diphosphate kinase in Pisum sativum L. cv. Alaska. J. Photochem. Photobiol. B: Biol. 45:1998;113-121.
    • (1998) J. Photochem. Photobiol. B: Biol. , vol.45 , pp. 113-121
    • Tanaka, N.1    Ogura, T.2    Noguchi, T.3    Hirano, H.4    Yabe, N.5    Hasunuma, K.6
  • 11
    • 0032567039 scopus 로고    scopus 로고
    • PIF3, a phytochrome-interacting factor necessary for normal photoinduced signal transduction, is a novel basic helix-loop-helix protein
    • Ni M., Tepperman J.M., Quail P.H. PIF3, a phytochrome-interacting factor necessary for normal photoinduced signal transduction, is a novel basic helix-loop-helix protein. Cell. 95:1998;657-667.
    • (1998) Cell , vol.95 , pp. 657-667
    • Ni, M.1    Tepperman, J.M.2    Quail, P.H.3
  • 14
    • 0022430790 scopus 로고
    • Isolation and characterization of soluble cytochromes, ferrodoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
    • Meyer T.E. Isolation and characterization of soluble cytochromes, ferrodoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila. Biochim. Biophys. Acta. 806:1985;175-183.
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 175-183
    • Meyer, T.E.1
  • 15
    • 0023152468 scopus 로고
    • Properties of a water-soluble, yellow protein isolated from a halophilic phototropic bacterium that has photochemical activity analogous to sensory rhodopsin
    • Meyer T.E., Yakali E., Cusanovich M.A., Tollin G. Properties of a water-soluble, yellow protein isolated from a halophilic phototropic bacterium that has photochemical activity analogous to sensory rhodopsin. Biochemistry. 26:1987;418-423.
    • (1987) Biochemistry , vol.26 , pp. 418-423
    • Meyer, T.E.1    Yakali, E.2    Cusanovich, M.A.3    Tollin, G.4
  • 17
    • 0029914630 scopus 로고    scopus 로고
    • Similarity among the Drosophila (6-4)photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family
    • Todo T., Ryo H., Yamamoto K., Toh H., Inui T., Ayaki H., Nomura T., Ikenaga M. Similarity among the Drosophila (6-4)photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family. Science. 272:1996;109-112.
    • (1996) Science , vol.272 , pp. 109-112
    • Todo, T.1    Ryo, H.2    Yamamoto, K.3    Toh, H.4    Inui, T.5    Ayaki, H.6    Nomura, T.7    Ikenaga, M.8
  • 18
    • 0029310457 scopus 로고
    • Characterization of a Chlamydomonas reinhardtii gene encoding a protein of the DNA photolyase/blue light photoreceptor family
    • Small G.D., Min B., Lefebvre P.A. Characterization of a Chlamydomonas reinhardtii gene encoding a protein of the DNA photolyase/blue light photoreceptor family. Plant Mol. Biol. 28:1995;443-454.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 443-454
    • Small, G.D.1    Min, B.2    Lefebvre, P.A.3
  • 19
    • 0032570771 scopus 로고    scopus 로고
    • Regulation of flowering time by Arabidopsis photoreceptors
    • Guo H., Yang H., Mockler T.C., Lin C. Regulation of flowering time by Arabidopsis photoreceptors. Science. 279:1998;1360-1363.
    • (1998) Science , vol.279 , pp. 1360-1363
    • Guo, H.1    Yang, H.2    Mockler, T.C.3    Lin, C.4
  • 20
    • 0032568457 scopus 로고    scopus 로고
    • Vitamin B2-based blue-light photoreceptors in the retinohypothalamic tract as the photoactive pigments for setting the circadian clock in mammal
    • Miyamoto Y., Sancar A. Vitamin B2-based blue-light photoreceptors in the retinohypothalamic tract as the photoactive pigments for setting the circadian clock in mammal. Proc. Natl. Acad. Sci. USA. 95:1998;6097-6102.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6097-6102
    • Miyamoto, Y.1    Sancar, A.2
  • 21
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phase
    • Pebay-Peyroula E., Rummel G., Rosenbusch J.P., Landau E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phase. Science. 277:1997;1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 25
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • Luecke H., Schobert B., Richter H.-T., Cartailler J.-P., Lanyi J.K. Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science. 286:1999;255-260.
    • (1999) Science , vol.286 , pp. 255-260
    • Luecke, H.1    Schobert, B.2    Richter, H.-T.3    Cartailler, J.-P.4    Lanyi, J.K.5
  • 26
    • 0026099851 scopus 로고
    • Fourier transform infrared studies of active-site-methylated rhodopsin. Implications for chromophore-protein interaction, transducin activation, and the reaction pathway
    • Ganter U.M., Longstaff C., Pajares M.A., Rando R.R., Siebert F. Fourier transform infrared studies of active-site-methylated rhodopsin. Implications for chromophore-protein interaction, transducin activation, and the reaction pathway. Biophys. J. 59:1991;640-644.
    • (1991) Biophys. J. , vol.59 , pp. 640-644
    • Ganter, U.M.1    Longstaff, C.2    Pajares, M.A.3    Rando, R.R.4    Siebert, F.5
  • 27
    • 0030810419 scopus 로고    scopus 로고
    • A distance measurement between specific sites on the cytoplasmic surface of bovine rhodopsin rod outer segment disk membranes
    • Albert A.D., Watts A., Spooner P., Groebner G., Young J., Yeagle P.L. A distance measurement between specific sites on the cytoplasmic surface of bovine rhodopsin rod outer segment disk membranes. Biochim. Biophys. Acta. 1328:1997;74-82.
    • (1997) Biochim. Biophys. Acta , vol.1328 , pp. 74-82
    • Albert, A.D.1    Watts, A.2    Spooner, P.3    Groebner, G.4    Young, J.5    Yeagle, P.L.6
  • 29
    • 0029110488 scopus 로고
    • 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • Borgstahl G.E., Williams D.R., Getzoff E.D. 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry. 34:1995;6278-6287.
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.1    Williams, D.R.2    Getzoff, E.D.3
  • 30
    • 0032510475 scopus 로고    scopus 로고
    • Structure at 0.85 Å resolution of an early protein photocycle intermediate
    • Genick U.K., Soltis S.M., Kuhn P., Canestrelli I.L., Getzoff E.D. Structure at 0.85 Å resolution of an early protein photocycle intermediate. Nature. 392:1998;206-209.
    • (1998) Nature , vol.392 , pp. 206-209
    • Genick, U.K.1    Soltis, S.M.2    Kuhn, P.3    Canestrelli, I.L.4    Getzoff, E.D.5
  • 32
    • 0032568630 scopus 로고    scopus 로고
    • Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily
    • Pellequer J.L., Wager-Smith K.A., Kay S.A., Getzoff E.D. Photoactive yellow protein: a structural prototype for the three-dimensional fold of the PAS domain superfamily. Proc. Natl. Acad. Sci. USA. 95:1998;5884-5890.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5884-5890
    • Pellequer, J.L.1    Wager-Smith, K.A.2    Kay, S.A.3    Getzoff, E.D.4
  • 33
    • 0032990441 scopus 로고    scopus 로고
    • PAS domain: Internal sensors of oxygen, redox potential, and light
    • Taylor B.L., Zhulin I.B. PAS domain: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:1999;479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 34
    • 0032872915 scopus 로고    scopus 로고
    • Remembrance of things PAS: Regulation of development by bHLH-PAS proteins
    • Crews S.T., Fan C.-M. Remembrance of things PAS: regulation of development by bHLH-PAS proteins. Curr. Opinion Genet. Development. 9:1999;580-587.
    • (1999) Curr. Opinion Genet. Development , vol.9 , pp. 580-587
    • Crews, S.T.1    Fan, C.-M.2
  • 35
    • 0033104316 scopus 로고    scopus 로고
    • Signalling pathways in two-component phosphorelay systems
    • Perraud A.L., Weiss V., Gross R. Signalling pathways in two-component phosphorelay systems. Trends Microbiol. 7:1999;115-120.
    • (1999) Trends Microbiol. , vol.7 , pp. 115-120
    • Perraud, A.L.1    Weiss, V.2    Gross, R.3
  • 36
    • 0030097470 scopus 로고    scopus 로고
    • Seeing blue: The discovery of cryptochrome
    • Ahmad M., Cashmore A.R. Seeing blue: the discovery of cryptochrome. Plant Mol. Biol. 30:1996;851-861.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 851-861
    • Ahmad, M.1    Cashmore, A.R.2
  • 37
    • 0029874444 scopus 로고    scopus 로고
    • No 'End of History' for photolyases
    • Sancar A. No 'End of History' for photolyases. Science. 272:1996;48-49.
    • (1996) Science , vol.272 , pp. 48-49
    • Sancar, A.1
  • 38
    • 0028117141 scopus 로고
    • Structure and function of DNA photolyase
    • Sancar A. Structure and function of DNA photolyase. Biochemistry. 33:1994;2-9.
    • (1994) Biochemistry , vol.33 , pp. 2-9
    • Sancar, A.1
  • 39
    • 0017748286 scopus 로고
    • Evidence for a sensitising pigment in fly photoreceptors
    • Kirschfeld K., Franceschini N., Minke B. Evidence for a sensitising pigment in fly photoreceptors. Nature. 269:1977;386-390.
    • (1977) Nature , vol.269 , pp. 386-390
    • Kirschfeld, K.1    Franceschini, N.2    Minke, B.3
  • 40
    • 0033013017 scopus 로고    scopus 로고
    • Enhanced retinal longwave sensitivity using a chlorophyll-derived photosensitiser in Malacosteus niger, a deep-sea dragon fish with far red bioluminescence
    • Douglas R.H., Partridge J.C., Dulai K.S., Hunt D.M., Mullineaux C.W., Hynninen P. Enhanced retinal longwave sensitivity using a chlorophyll-derived photosensitiser in Malacosteus niger, a deep-sea dragon fish with far red bioluminescence. Vision Res. 39:1999;2817-2832.
    • (1999) Vision Res. , vol.39 , pp. 2817-2832
    • Douglas, R.H.1    Partridge, J.C.2    Dulai, K.S.3    Hunt, D.M.4    Mullineaux, C.W.5    Hynninen, P.6
  • 41
    • 0026334916 scopus 로고
    • Determination of rates and yields of interchromophore (folate-flavin) energy transfer and intermolecular (flavin-DNA) electron transfer in Escherichia coli photolyase by time-resolved fluorescence and absorption spectroscopy
    • Kim S.T., Heelis P.F., Okamura T., Hirata Y., Mataga N., Sancar A. Determination of rates and yields of interchromophore (folate-flavin) energy transfer and intermolecular (flavin-DNA) electron transfer in Escherichia coli photolyase by time-resolved fluorescence and absorption spectroscopy. Biochemistry. 30:1991;11262-11270.
    • (1991) Biochemistry , vol.30 , pp. 11262-11270
    • Kim, S.T.1    Heelis, P.F.2    Okamura, T.3    Hirata, Y.4    Mataga, N.5    Sancar, A.6
  • 44
    • 0033617475 scopus 로고    scopus 로고
    • Cryptochromes: Blue light receptors for plants and animals
    • Cashmore A.R., Jarillo J.A., Wu Y.J., Liu D. Cryptochromes: blue light receptors for plants and animals. Science. 284:1999;760-765.
    • (1999) Science , vol.284 , pp. 760-765
    • Cashmore, A.R.1    Jarillo, J.A.2    Wu, Y.J.3    Liu, D.4
  • 46
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page C.C., Moser C.C., Chen X., Dutton P.L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature. 402:1999;47.
    • (1999) Nature , vol.402 , pp. 47
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 47
    • 0002413436 scopus 로고
    • Modern Quantum Chemistry
    • in: O. Sinanoglu (Ed.), Academic Press, New York
    • T. Förster, in: O. Sinanoglu (Ed.), Modern Quantum Chemistry, Part III, Action of Light and Organic Molecules, Academic Press, New York, 1965, pp. 93-137.
    • (1965) Action of Light and Organic Molecules , Issue.3 PART , pp. 93-137
    • Förster, T.1
  • 48
    • 0029061519 scopus 로고
    • Putative blue-light photoreceptors from Arabidopsis thaliana and Sinapis alba with a high degree of sequence homology to DNA photolyase contain the two photolyase cofactors but lack DNA repair activity
    • Malhotra K., Kim S.T., Batschauer A., Dawut L., Sancar A. Putative blue-light photoreceptors from Arabidopsis thaliana and Sinapis alba with a high degree of sequence homology to DNA photolyase contain the two photolyase cofactors but lack DNA repair activity. Biochemistry. 34:1995;6892-6899.
    • (1995) Biochemistry , vol.34 , pp. 6892-6899
    • Malhotra, K.1    Kim, S.T.2    Batschauer, A.3    Dawut, L.4    Sancar, A.5
  • 53
    • 0033580921 scopus 로고    scopus 로고
    • Protonation/deprotonation reactions triggered by photoactivation of photoactive yellow protein from Ectothiorhodospira halophilia
    • Hendriks J., Hoff W.D., Crielaard W., Hellingwerf K.J. Protonation/deprotonation reactions triggered by photoactivation of photoactive yellow protein from Ectothiorhodospira halophilia. J. Biol. Chem. 274:1999;17655-17661.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17655-17661
    • Hendriks, J.1    Hoff, W.D.2    Crielaard, W.3    Hellingwerf, K.J.4
  • 54
    • 0032857645 scopus 로고    scopus 로고
    • Kinetics of and intermediates in a photocycle branching reaction of the photoactive yellow protein from Ectothiorhodospira halophilia
    • Hendriks J., van Stokkum I.H.M., Crielaard W., Hellingwerf K.J. Kinetics of and intermediates in a photocycle branching reaction of the photoactive yellow protein from Ectothiorhodospira halophilia. FEBS Lett. 458:1999;252-256.
    • (1999) FEBS Lett. , vol.458 , pp. 252-256
    • Hendriks, J.1    Van Stokkum, I.H.M.2    Crielaard, W.3    Hellingwerf, K.J.4
  • 55
    • 0026331216 scopus 로고
    • Identification of signalling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: The case of sensory rhodopsin II
    • Yan B., Takahashi T., Johnson R., Spudich J.L. Identification of signalling states of a sensory receptor by modulation of lifetimes of stimulus-induced conformations: the case of sensory rhodopsin II. Biochemistry. 30:1991;10686-10692.
    • (1991) Biochemistry , vol.30 , pp. 10686-10692
    • Yan, B.1    Takahashi, T.2    Johnson, R.3    Spudich, J.L.4
  • 58
    • 0031772265 scopus 로고    scopus 로고
    • The phenolic recognition profiles of the Agrobacterium tumefaciens VirA protein are broadened by a high level of the sugar binding protein ChvE
    • Peng W.-T., Lee Y.-W., Nester E.W. The phenolic recognition profiles of the Agrobacterium tumefaciens VirA protein are broadened by a high level of the sugar binding protein ChvE. J. Bacteriol. 180:1998;5632-5638.
    • (1998) J. Bacteriol. , vol.180 , pp. 5632-5638
    • Peng, W.-T.1    Lee, Y.-W.2    Nester, E.W.3
  • 59
    • 0032033681 scopus 로고    scopus 로고
    • Three-state and two-state models
    • Strange P.G. Three-state and two-state models. Trends Pharmacol. Sci. 19:1998;85-86.
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 85-86
    • Strange, P.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.