메뉴 건너뛰기




Volumn 49, Issue 1, 2007, Pages 4-10

Phototropins and their LOV domains: Versatile plant blue-light receptors

Author keywords

Blue light receptor; Flavin cysteinyl adduct; LOV domain; Phototropin; Phototropism

Indexed keywords

CHLOROPLAST; PHOTOAUTOTROPHY; PHOTORECEPTION; PLANT; STOMATA;

EID: 33846120456     PISSN: 16729072     EISSN: 17447909     Source Type: Journal    
DOI: 10.1111/j.1744-7909.2006.00406.x     Document Type: Review
Times cited : (29)

References (43)
  • 1
    • 0027493250 scopus 로고
    • HY4 gene of A. thaliana encodes a protein with the characteristics of a blue-light photoreceptor
    • Ahmad A, Cashmore AR (1993). HY4 gene of A. thaliana encodes a protein with the characteristics of a blue-light photoreceptor. Nature 366, 162-166.
    • (1993) Nature , vol.366 , pp. 162-166
    • Ahmad, A.1    Cashmore, A.R.2
  • 2
    • 84889366079 scopus 로고    scopus 로고
    • Plant cryptochromes: Their genes, biochemistry, and physiological roles
    • In: Briggs WR, Spudich JL, eds. Wiley VCH, Weinheim
    • Batschauer A (2005). Plant cryptochromes: Their genes, biochemistry, and physiological roles. In: Briggs WR, Spudich JL, eds. Handbook of Photosensory Receptors. Wiley VCH, Weinheim. pp. 211-258.
    • (2005) Handbook of Photosensory Receptors , pp. 211-258
    • Batschauer, A.1
  • 3
    • 84920141932 scopus 로고    scopus 로고
    • Blue/UV-A receptors: Historical overview
    • In: Schäfer E, Nagy F, eds. Third Edition, Function and Signal Transduction Mechanisms. Springer, Dorcrecht
    • Briggs WR (2006). Blue/UV-A receptors: Historical overview. In: Schäfer E, Nagy F, eds. Photomorphogenesis in Plants and Bacteria, Third Edition, Function and Signal Transduction Mechanisms. Springer, Dorcrecht. pp. 171-197.
    • (2006) Photomorphogenesis in Plants and Bacteria , pp. 171-197
    • Briggs, W.R.1
  • 5
    • 0035208894 scopus 로고    scopus 로고
    • Phototropins: A new family of flavin-binding blue light receptors in plants
    • Briggs WR, Christie JM, Salomon M (2001b). Phototropins: A new family of flavin-binding blue light receptors in plants. Antiox Redox Signaling 3, 775-788.
    • (2001) Antiox Redox Signaling , vol.3 , pp. 775-788
    • Briggs, W.R.1    Christie, J.M.2    Salomon, M.3
  • 6
    • 14744276473 scopus 로고    scopus 로고
    • Phototropins and associated signaling: Providing the power of movement in higher plants
    • Celaya RB, Liscum E (2005). Phototropins and associated signaling: Providing the power of movement in higher plants. Photochem Photobiol 81, 73-80.
    • (2005) Photochem Photobiol , vol.81 , pp. 73-80
    • Celaya, R.B.1    Liscum, E.2
  • 8
    • 84889309479 scopus 로고    scopus 로고
    • Blue light sensing and signaling by the phototropins
    • In: Briggs WR, Spudich JL, eds. Wiley VCH, Weinheim
    • Christie JM, Briggs WR (2005). Blue light sensing and signaling by the phototropins. In: Briggs WR, Spudich JL, eds. Handbook of Photosensory Receptors. Wiley VCH, Weinheim. pp. 277-303.
    • (2005) Handbook of Photosensory Receptors , pp. 277-303
    • Christie, J.M.1    Briggs, W.R.2
  • 9
    • 0032573502 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A flavoprotein with the properties of a photoreceptor for phototropism
    • Christie JM, Reymond P, Powell GK, Bernasconi P, Raibekas AA, Liscum E et al. (1998). Arabidopsis NPH1: A flavoprotein with the properties of a photoreceptor for phototropism. Science 282, 1698-1701.
    • (1998) Science , vol.282 , pp. 1698-1701
    • Christie, J.M.1    Reymond, P.2    Powell, G.K.3    Bernasconi, P.4    Raibekas, A.A.5    Liscum, E.6
  • 10
    • 0033587744 scopus 로고    scopus 로고
    • LOV (light, oxygen, voltage) domains of the blue-light photore-ceptor (nph1): Binding sites for the chromophore flavin mononucleotide
    • Christie JM, Salomon M, Nozue K, Wada M, Briggs WR (1999). LOV (light, oxygen, voltage) domains of the blue-light photore-ceptor (nph1): Binding sites for the chromophore flavin mononucleotide. Proc Natl Acad Sci USA 96, 8779-8783.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8779-8783
    • Christie, J.M.1    Salomon, M.2    Nozue, K.3    Wada, M.4    Briggs, W.R.5
  • 11
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • Christie JM, Swartz TE, Bogomolni R, Briggs WR (2002). Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function. Plant J 32, 205-219.
    • (2002) Plant J , vol.32 , pp. 205-219
    • Christie, J.M.1    Swartz, T.E.2    Bogomolni, R.3    Briggs, W.R.4
  • 12
    • 0037428497 scopus 로고    scopus 로고
    • Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1
    • Corchnoy SB, Swartz TE, Lewis JW, Szundi I, Briggs WR, Bogomolni R (2003). Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1. J Biol Chem 278, 724-731.
    • (2003) J Biol Chem , vol.278 , pp. 724-731
    • Corchnoy, S.B.1    Swartz, T.E.2    Lewis, J.W.3    Szundi, I.4    Briggs, W.R.5    Bogomolni, R.6
  • 13
    • 33846063572 scopus 로고    scopus 로고
    • LOV-domain structure, dynamics, and diversity
    • In: Briggs WR, Spudich JL, eds. Wiley VCH, Weinheim
    • Crosson S (2005). LOV-domain structure, dynamics, and diversity. In: Briggs WR, Spudich JL, eds. Handbook of Photosensory Receptors. Wiley VCH, Weinheim. pp. 323-336.
    • (2005) Handbook of Photosensory Receptors , pp. 323-336
    • Crosson, S.1
  • 14
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson S, Moffat K (2001). Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction. Proc Natl Acad Sci USA 98, 2995-3000.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 15
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson S, Moffat K (2002). Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch. Plant Cell 14, 1067-1075.
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 16
    • 0037008528 scopus 로고    scopus 로고
    • White collar-1, a circadian blue light photoreceptor, binding to the frequency promoter
    • Froelich AC, Liu Y, Loros JJ, Dunlap JC (2002). White collar-1, a circadian blue light photoreceptor, binding to the frequency promoter. Science 297, 815-819.
    • (2002) Science , vol.297 , pp. 815-819
    • Froelich, A.C.1    Liu, Y.2    Loros, J.J.3    Dunlap, J.C.4
  • 17
    • 0000258296 scopus 로고
    • Light-mediated changes in two proteins found associated with plasma membrane fractions from pea stem sections
    • Gallagher S, Short TW, Ray PM, Pratt LH, Briggs WR (1988). Light-mediated changes in two proteins found associated with plasma membrane fractions from pea stem sections. Proc Natl Acad Sci USA 85, 8003-8007.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8003-8007
    • Gallagher, S.1    Short, T.W.2    Ray, P.M.3    Pratt, L.H.4    Briggs, W.R.5
  • 18
    • 11144344967 scopus 로고    scopus 로고
    • Disruption of the LOV/Jα helix interaction activates phototropin kinase activity
    • Harper SM, Christie JM, Gardner KH (2004). Disruption of the LOV/ Jα helix interaction activates phototropin kinase activity. Biochemistry 43, 16184-16192.
    • (2004) Biochemistry , vol.43 , pp. 16184-16192
    • Harper, S.M.1    Christie, J.M.2    Gardner, K.H.3
  • 19
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper SM, Neil LC, Gardner KH (2003). Structural basis of a phototropin light switch. Science 301, 1541-1544.
    • (2003) Science , vol.301 , pp. 1541-1544
    • Harper, S.M.1    Neil, L.C.2    Gardner, K.H.3
  • 20
    • 0029857950 scopus 로고    scopus 로고
    • PHH1, a novel gene from Arabidopsis thaliana that encodes a protein similar to plant blue-light photoreceptors and microbial photolyases
    • Hoffman PD, Batschauer A, Hays JB (1996). PHH1, a novel gene from Arabidopsis thaliana that encodes a protein similar to plant blue-light photoreceptors and microbial photolyases. Mol Gen Genet 253, 259-265.
    • (1996) Mol Gen Genet , vol.253 , pp. 259-265
    • Hoffman, P.D.1    Batschauer, A.2    Hays, J.B.3
  • 21
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative re-dox-sensing domain
    • Huala E, Oeller PW, Liscum E, Han IS, Larsen E, Briggs WR (1997). Arabidopsis NPH1: A protein kinase with a putative re-dox-sensing domain. Science 278, 2120-2123.
    • (1997) Science , vol.278 , pp. 2120-2123
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.S.4    Larsen, E.5    Briggs, W.R.6
  • 22
    • 0037687415 scopus 로고    scopus 로고
    • Phototropin is the blue-light receptor that controls multiple steps in the sexual life cycle of the green alga Chlamydomonas reinhardtii
    • Huang K, Beck CF (2003). Phototropin is the blue-light receptor that controls multiple steps in the sexual life cycle of the green alga Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 100, 6269-6274.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6269-6274
    • Huang, K.1    Beck, C.F.2
  • 23
    • 17844395528 scopus 로고    scopus 로고
    • Light controls growth and development via a conserved pathway in the fungal kingdom
    • Idnurm A, Heitman J (2005). Light controls growth and development via a conserved pathway in the fungal kingdom. PLoS Biol 3, 615-626.
    • (2005) PLoS Biol , vol.3 , pp. 615-626
    • Idnurm, A.1    Heitman, J.2
  • 24
    • 33645236535 scopus 로고    scopus 로고
    • The Phycomyces madA gene encodes a blue-light photoreceptor for phototropism and other light responses
    • Idnurm A, Rodriguez J, Corrochano L, Sanz C, Iturriaga EA, Eslavo AP et al. (2006). The Phycomyces madA gene encodes a blue-light photoreceptor for phototropism and other light responses. Proc Natl Acad Sci USA 103, 4546-4551.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4546-4551
    • Idnurm, A.1    Rodriguez, J.2    Corrochano, L.3    Sanz, C.4    Iturriaga, E.A.5    Eslavo, A.P.6
  • 25
    • 2342541694 scopus 로고    scopus 로고
    • Function analysis of phototropin2 using fern mutants deficient in blue light-induced chloroplast avoidance movement
    • Kagawa T, Kasahara M, Abe T, Yoshida S, Wada M (2004). Function analysis of phototropin2 using fern mutants deficient in blue light-induced chloroplast avoidance movement. Plant Cell Physiol 45, 416-426.
    • (2004) Plant Cell Physiol , vol.45 , pp. 416-426
    • Kagawa, T.1    Kasahara, M.2    Abe, T.3    Yoshida, S.4    Wada, M.5
  • 26
    • 0035983657 scopus 로고    scopus 로고
    • Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii
    • Kasahara M, Swartz TE, Olney MA, Onodera A, Muchizuki N, Fukuzawa H et al. (2002). Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii. Plant Physiol 129, 762-773.
    • (2002) Plant Physiol , vol.129 , pp. 762-773
    • Kasahara, M.1    Swartz, T.E.2    Olney, M.A.3    Onodera, A.4    Muchizuki, N.5    Fukuzawa, H.6
  • 28
    • 0001078531 scopus 로고    scopus 로고
    • CRY2: A second member of the Arabidopsis cryptochrome family (Accession No. U43397). Plant Gene Register PGR96-001
    • Lin C, Ahmad M, Chan J, Cashmore AR (1996). CRY2: A second member of the Arabidopsis cryptochrome family (Accession No. U43397). Plant Gene Register PGR96-001. Plant Physiol 110, 1047.
    • (1996) Plant Physiol , vol.110 , pp. 1047
    • Lin, C.1    Ahmad, M.2    Chan, J.3    Cashmore, A.R.4
  • 29
    • 0029278701 scopus 로고
    • Mutations in the NPH1 locus of Arabidopsis disrupt perception of phototropic stimuli
    • Liscum E, Briggs WR (1995). Mutations in the NPH1 locus of Arabidopsis disrupt perception of phototropic stimuli. Plant Cell 7, 473-485.
    • (1995) Plant Cell , vol.7 , pp. 473-485
    • Liscum, E.1    Briggs, W.R.2
  • 30
    • 3242747589 scopus 로고    scopus 로고
    • The bacterial counterparts of plant phototropins
    • Losi A (2004). The bacterial counterparts of plant phototropins. Photochem Photobiol Sci 3, 566-574.
    • (2004) Photochem Photobiol Sci , vol.3 , pp. 566-574
    • Losi, A.1
  • 31
    • 0036224807 scopus 로고    scopus 로고
    • First evidence for phototropin-related blue-light receptors in prokaryotes
    • Losi A, Polverini E, Quest B, Gärtner W (2002). First evidence for phototropin-related blue-light receptors in prokaryotes. Biophys J 82, 2627-2634.
    • (2002) Biophys J , vol.82 , pp. 2627-2634
    • Losi, A.1    Polverini, E.2    Quest, B.3    Gärtner, W.4
  • 32
    • 24944553332 scopus 로고    scopus 로고
    • Blue light-regulated molecular switch of ser/thr/kinas in phototropin
    • Matsuoka D, Tokutomi S (2005). Blue light-regulated molecular switch of ser/thr/kinas in phototropin. Proc Natl Acad Sci USA 102, 13337-13342.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13337-13342
    • Matsuoka, D.1    Tokutomi, S.2
  • 33
    • 0025363920 scopus 로고
    • Use of a site-directed triple mutant to trap intermediates: Demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase
    • Miller SM, Massey V, Ballou D, Williams CH Jr, Distefano M, Moore MJ et al. (1980). Use of a site-directed triple mutant to trap intermediates: Demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase. Biochemistry 29, 2831-2841.
    • (1980) Biochemistry , vol.29 , pp. 2831-2841
    • Miller, S.M.1    Massey, V.2    Ballou, D.3    Williams Jr., C.H.4    Distefano, M.5    Moore, M.J.6
  • 34
    • 33745443340 scopus 로고
    • Della influenza che ha il raggio magnetico sulla vegetazione delle piante
    • (in Italian)
    • Poggioli S (1817). Della influenza che ha il raggio magnetico sulla vegetazione delle piante. Bologna-Coi Tipi di Annesio nobili Opusc Scientif Fasc, 1 9-23 (in Italian).
    • (1817) Bologna-Coi Tipi Di Annesio Nobili Opusc Scientif Fasc , vol.1 , pp. 9-23
    • Poggioli, S.1
  • 35
    • 0029257361 scopus 로고
    • Involvement of thiol groups in blue light-induced phosphorylation of a plasma membrane-associated protein from coleoptile tips of Zea mays L
    • Rüdiger W, Briggs WR (1995). Involvement of thiol groups in blue light-induced phosphorylation of a plasma membrane-associated protein from coleoptile tips of Zea mays L. Zeit Naturforsch 50c, 231-234.
    • (1995) Zeit Naturforsch , vol.50 c , pp. 231-234
    • Rüdiger, W.1    Briggs, W.R.2
  • 36
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor phototropin
    • Salomon M, Christie JM, Knieb E, Lempert U, Briggs WR (2000). Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor phototropin. Biochemistry 39, 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 37
    • 4143081643 scopus 로고    scopus 로고
    • Dimerizatiuon of the plant photoreceptor phototropin is probably mediated by the LOV1 domain
    • Salomon M, Lempert U, Rüdiger W (2004). Dimerizatiuon of the plant photoreceptor phototropin is probably mediated by the LOV1 domain. FEBS Lett 572, 8-10.
    • (2004) FEBS Lett , vol.572 , pp. 8-10
    • Salomon, M.1    Lempert, U.2    Rüdiger, W.3
  • 38
    • 33846044486 scopus 로고    scopus 로고
    • The ZEITLUPE family of putative photoreceptors
    • In: Briggs WR, Spudich JL, eds. Wiley VCH, Weinheim
    • Schultz TF (2005). The ZEITLUPE family of putative photoreceptors. In: Briggs WR, Spudich JL, eds. Handbook of Photosensory Receptors. Wiley VCH, Weinheim. pp. 337-347.
    • (2005) Handbook of Photosensory Receptors , pp. 337-347
    • Schultz, T.F.1
  • 39
    • 0141848660 scopus 로고    scopus 로고
    • VIVID is a flavoprotein and serves as a fungal blue light photoreceptor for photoadaptation
    • Schwerdtfeger C, Linden H (2003). VIVID is a flavoprotein and serves as a fungal blue light photoreceptor for photoadaptation. EMBO J 22, 4846-4855.
    • (2003) EMBO J , vol.22 , pp. 4846-4855
    • Schwerdtfeger, C.1    Linden, H.2
  • 40
    • 0037173051 scopus 로고    scopus 로고
    • Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamy-domonas reinhardtii
    • Sineshchekov O, Jung KH, Spudich JL (2002). Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamy-domonas reinhardtii. Proc Natl Acad Sci USA 99, 8689-8694.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8689-8694
    • Sineshchekov, O.1    Jung, K.H.2    Spudich, J.L.3
  • 41
  • 42
    • 0037062577 scopus 로고    scopus 로고
    • Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domains of the plant blue-light receptor phototropin 1
    • Swartz TE, Wenzel PJ, Corchnoy SB, Briggs WR, Bogomolni R (2002). Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domains of the plant blue-light receptor phototropin 1. Biochemistry 41, 7183-7189.
    • (2002) Biochemistry , vol.41 , pp. 7183-7189
    • Swartz, T.E.1    Wenzel, P.J.2    Corchnoy, S.B.3    Briggs, W.R.4    Bogomolni, R.5
  • 43
    • 0027137014 scopus 로고
    • Blue light-induced phosphoryla-tion of a plasma membrane protein in pea: A step in the signal transduction chain for phototropism
    • Warpeha KMF, Briggs WR (1993). Blue light-induced phosphoryla-tion of a plasma membrane protein in pea: A step in the signal transduction chain for phototropism. Aust J Plant Physiol 20, 393-403.
    • (1993) Aust J Plant Physiol , vol.20 , pp. 393-403
    • Warpeha, K.M.F.1    Briggs, W.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.