메뉴 건너뛰기




Volumn 111, Issue 14, 2014, Pages 5219-5224

On the mechanism of photoinduced dimer dissociation in the plant UVR8 photoreceptor

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; MONOMER; SODIUM CHLORIDE; TRYPTOPHAN; UNCLASSIFIED DRUG; UVR8 PROTEIN; VEGETABLE PROTEIN;

EID: 84992111030     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1402025111     Document Type: Article
Times cited : (32)

References (44)
  • 1
    • 0036742711 scopus 로고    scopus 로고
    • Arabidopsis UVR8 regulates ultraviolet-B signal transduction and tolerance and contains sequence similarity to human regulator of chromatin condensation
    • Kliebenstein DJ, Lim JE, Landry LG, Last RL (2002) Arabidopsis UVR8 regulates ultraviolet-B signal transduction and tolerance and contains sequence similarity to human regulator of chromatin condensation Plant Physiol 130(1):234-243
    • (2002) Plant Physiol , vol.130 , Issue.1 , pp. 234-243
    • Kliebenstein, D.J.1    Lim, J.E.2    Landry, L.G.3    Last, R.L.4
  • 2
    • 35348841586 scopus 로고    scopus 로고
    • UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific signaling component UVR8 and activates its function in the nucleus
    • Kaiserli E, Jenkins GI (2007) UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific signaling component UVR8 and activates its function in the nucleus. Plant Cell 19(8):2662-2673.
    • (2007) Plant Cell , vol.19 , Issue.8 , pp. 2662-2673
    • Kaiserli, E.1    Jenkins, G.I.2
  • 3
    • 66449126361 scopus 로고    scopus 로고
    • Signal transduction in responses to UV-B radiation
    • Jenkins GI (2009) Signal transduction in responses to UV-B radiation. Annu Rev Plant Biol 60:407-431.
    • (2009) Annu Rev Plant Biol , vol.60 , pp. 407-431
    • Jenkins, G.I.1
  • 4
    • 29144433413 scopus 로고    scopus 로고
    • A UV-B-specific signaling component orchestrates plant UV protection
    • Brown BA, et al. (2005) A UV-B-specific signaling component orchestrates plant UV protection. Proc Natl Acad Sci USA 102(50):18225-18230.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.50 , pp. 18225-18230
    • Brown, B.A.1
  • 5
    • 58549113569 scopus 로고    scopus 로고
    • Role of root UV-B sensing in Arabidopsis early seedling development
    • Tong HY, et al. (2008) Role of root UV-B sensing in Arabidopsis early seedling development. Proc Natl Acad Sci USA 105(52):21039-21044.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.52 , pp. 21039-21044
    • Tong, H.Y.1
  • 6
    • 84859646883 scopus 로고    scopus 로고
    • UV-B photoreceptor-mediated signalling in plants
    • Heijde M, Ulm R (2012) UV-B photoreceptor-mediated signalling in plants. Trends Plant Sci 17(4):230-237.
    • (2012) Trends Plant Sci , vol.17 , Issue.4 , pp. 230-237
    • Heijde, M.1    Ulm, R.2
  • 7
    • 84868159269 scopus 로고    scopus 로고
    • In vivo function of tryptophans in the Arabidopsis UV-B photoreceptor UVR8
    • O'Hara A, Jenkins GI (2012) In vivo function of tryptophans in the Arabidopsis UV-B photoreceptor UVR8. Plant Cell 24(9):3755-3766.
    • (2012) Plant Cell , vol.24 , Issue.9 , pp. 3755-3766
    • O'hara, A.1    Jenkins, G.I.2
  • 8
    • 84863393216 scopus 로고    scopus 로고
    • Plant UVR8 photoreceptor senses UV-B by tryptophanmediated disruption of cross-dimer salt bridges
    • Christie JM, et al. (2012) Plant UVR8 photoreceptor senses UV-B by tryptophanmediated disruption of cross-dimer salt bridges. Science 335(6075):1492-1496.
    • (2012) Science , vol.335 , Issue.6075 , pp. 1492-1496
    • Christie, J.M.1
  • 9
    • 84862776742 scopus 로고    scopus 로고
    • Structural basis of ultraviolet-B perception by UVR8
    • Wu D, et al. (2012) Structural basis of ultraviolet-B perception by UVR8. Nature 484(7393):214-219.
    • (2012) Nature , vol.484 , Issue.7393 , pp. 214-219
    • Wu, D.1
  • 10
    • 79953272725 scopus 로고    scopus 로고
    • Perception of UV-B by the Arabidopsis UVR8 protein
    • Rizzini L, et al. (2011) Perception of UV-B by the Arabidopsis UVR8 protein. Science 332(6025):103-106.
    • (2011) Science , vol.332 , Issue.6025 , pp. 103-106
    • Rizzini, L.1
  • 11
    • 34547397574 scopus 로고    scopus 로고
    • Lightening up the UV response by identification of the arylhydrocarbon receptor as a cytoplasmatic target for ultraviolet B radiation
    • Fritsche E, et al. (2007) Lightening up the UV response by identification of the arylhydrocarbon receptor as a cytoplasmatic target for ultraviolet B radiation. Proc Natl Acad Sci USA 104(21):8851-8856.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.21 , pp. 8851-8856
    • Fritsche, E.1
  • 12
    • 69649088670 scopus 로고    scopus 로고
    • UV-B action spectrum for UVR8-mediated HY5 transcript accumulation in Arabidopsis
    • Brown BA, Headland LR, Jenkins GI (2009) UV-B action spectrum for UVR8-mediated HY5 transcript accumulation in Arabidopsis. Photochem Photobiol 85(5):1147-1155.
    • (2009) Photochem Photobiol , vol.85 , Issue.5 , pp. 1147-1155
    • Brown, B.A.1    Headland, L.R.2    Jenkins, G.I.3
  • 13
    • 84867036845 scopus 로고    scopus 로고
    • C-terminal region of the UV-B photoreceptor UVR8 initiates signaling through interaction with the COP1 protein
    • Cloix C, et al. (2012) C-terminal region of the UV-B photoreceptor UVR8 initiates signaling through interaction with the COP1 protein. Proc Natl Acad Sci USA 109(40): 16366-16370.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.40 , pp. 16366-16370
    • Cloix, C.1
  • 14
    • 84874964240 scopus 로고    scopus 로고
    • Reversion of the Arabidopsis UV-B photoreceptor UVR8 to the homodimeric ground state
    • Heijde M, Ulm R (2013) Reversion of the Arabidopsis UV-B photoreceptor UVR8 to the homodimeric ground state. Proc Natl Acad Sci USA 110(3):1113-1118.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.3 , pp. 1113-1118
    • Heijde, M.1    Ulm, R.2
  • 15
    • 78650571336 scopus 로고    scopus 로고
    • Negative feedback regulation of UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis
    • Gruber H, et al. (2010) Negative feedback regulation of UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis. Proc Natl Acad Sci USA 107(46): 20132-20137.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.46 , pp. 20132-20137
    • Gruber, H.1
  • 16
    • 84877783598 scopus 로고    scopus 로고
    • Ultraviolet-B-mediated induction of protein-protein interactions in mammalian cells
    • Crefcoeur RP, Yin R, Ulm R, Halazonetis TD (2013) Ultraviolet-B-mediated induction of protein-protein interactions in mammalian cells. Nat Commun 4:1779.
    • (2013) Nat Commun , vol.4 , pp. 1779
    • Crefcoeur, R.P.1    Yin, R.2    Ulm, R.3    Halazonetis, T.D.4
  • 17
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui Q, Karplus M (2008) Allostery and cooperativity revisited. Protein Sci 17(8): 1295-1307.
    • (2008) Protein Sci , vol.17 , Issue.8 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 18
    • 82955169516 scopus 로고    scopus 로고
    • Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-β Structure of Aβ(42) amyloid aggregates
    • Mithu VS, et al. (2011) Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-β Structure of Aβ(42) amyloid aggregates. Biophys J 101(11):2825-2832.
    • (2011) Biophys J , vol.101 , Issue.11 , pp. 2825-2832
    • Mithu, V.S.1
  • 19
    • 84891753192 scopus 로고    scopus 로고
    • Quenching dynamics of ultraviolet-light perception by UVR8 photoreceptor
    • Liu Z, et al. (2014) Quenching dynamics of ultraviolet-light perception by UVR8 photoreceptor. J Phys Chem Lett 5(1):69-72.
    • (2014) J Phys Chem Lett , vol.5 , Issue.1 , pp. 69-72
    • Liu, Z.1
  • 20
    • 84880534992 scopus 로고    scopus 로고
    • Interactions and stabilities of the UV RESISTANCE LOCUS8 (UVR8) protein dimer and its key mutants
    • Wu M, Strid A, Eriksson LA (2013) Interactions and stabilities of the UV RESISTANCE LOCUS8 (UVR8) protein dimer and its key mutants. J Chem Inf Model 53(7): 1736-1746.
    • (2013) J Chem Inf Model , vol.53 , Issue.7 , pp. 1736-1746
    • Wu, M.1    Strid, A.2    Eriksson, L.A.3
  • 21
    • 83455224906 scopus 로고    scopus 로고
    • Essential on the photophysics and photochemistry of the indole chromophore by using a totally unconstrained theoretical approach
    • Giussani A, Merchan M, Roca-Sanjuan D, Lindh R (2011) Essential on the photophysics and photochemistry of the indole chromophore by using a totally unconstrained theoretical approach. J Chem Theory Comput 7(12):4088-4096.
    • (2011) J Chem Theory Comput , vol.7 , Issue.12 , pp. 4088-4096
    • Giussani, A.1    Merchan, M.2    Roca-Sanjuan, D.3    Lindh, R.4
  • 22
    • 0030610813 scopus 로고    scopus 로고
    • 1La and 1Lb transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins
    • Callis PR (1997) 1La and 1Lb transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol 278: 113-150.
    • (1997) Methods Enzymol , vol.278 , pp. 113-150
    • Callis, P.R.1
  • 23
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky TJ, et al. (2007) PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res 35(Web Server issue):W522-W555.
    • (2007) Nucleic Acids Res , vol.35 , Issue.WEB SERVER ISSUE.
    • Dolinsky, T.J.1
  • 24
    • 66049120630 scopus 로고    scopus 로고
    • Ultrafast quenching of TRP fluorescence in proteins: Interresidue and intrahelical electron transfer
    • Qiu W, et al. (2008) Ultrafast quenching of TRP fluorescence in proteins: Interresidue and intrahelical electron transfer. Chem Phys 350(1-3):154-164.
    • (2008) Chem Phys , vol.350 , Issue.1-3 , pp. 154-164
    • Qiu, W.1
  • 25
    • 65249138942 scopus 로고    scopus 로고
    • Solvent effects on the fluorescence quenching of tryptophan by amides via electron transfer
    • Muiño PL, Callis PR (2009) Solvent effects on the fluorescence quenching of tryptophan by amides via electron transfer. Experimental and computational studies. J Phys Chem B 113(9):2572-2577.
    • (2009) Experimental and Computational Studies. J Phys Chem B , vol.113 , Issue.9 , pp. 2572-2577
    • Muiño, P.L.1    Callis, P.R.2
  • 26
    • 33750193907 scopus 로고
    • Thermal electron transfer reactions in polar solvents
    • Kestner NR, Logan J, Jortner J (1974) Thermal electron transfer reactions in polar solvents. J Phys Chem 78(21):2148-2166.
    • (1974) J Phys Chem , vol.78 , Issue.21 , pp. 2148-2166
    • Kestner, N.R.1    Logan, J.2    Jortner, J.3
  • 27
    • 4243234418 scopus 로고    scopus 로고
    • Calculation of electronic coupling matrix elements for ground and excited state electron transfer reactions: Comparison of the Generalized Mulliken-Hush and block diagonalization methods
    • Cave RJ, Newton MD (1997) Calculation of electronic coupling matrix elements for ground and excited state electron transfer reactions: Comparison of the Generalized Mulliken-Hush and block diagonalization methods. J Chem Phys 106(22):9213-9226.
    • (1997) J Chem Phys , vol.106 , Issue.22 , pp. 9213-9226
    • Cave, R.J.1    Newton, M.D.2
  • 28
    • 0037159077 scopus 로고    scopus 로고
    • Fragment charge difference method for estimating donor-acceptor electronic coupling. Application to DNA π-stacks
    • Voityuk AA, Rösch N (2002) Fragment charge difference method for estimating donor-acceptor electronic coupling. Application to DNA π-stacks. J Chem Phys 117(12): 5607-5616.
    • (2002) J Chem Phys , vol.117 , Issue.12 , pp. 5607-5616
    • Voityuk, A.A.1    Rösch, N.2
  • 29
    • 84873970937 scopus 로고    scopus 로고
    • Estimation of electronic coupling for photoinduced chargeseparation and charge recombination using the fragment charge difference method
    • Voityuk AA (2013) Estimation of electronic coupling for photoinduced chargeseparation and charge recombination using the fragment charge difference method. J Phys Chem C 117(6):2670-2675.
    • (2013) J Phys Chem C , vol.117 , Issue.6 , pp. 2670-2675
    • Voityuk, A.A.1
  • 30
    • 38949210653 scopus 로고    scopus 로고
    • Quantifying free energy profiles of proton transfer reactions in solution and proteins by using a diabatic FDFT mapping
    • Xiang Y, Warshel A (2008) Quantifying free energy profiles of proton transfer reactions in solution and proteins by using a diabatic FDFT mapping. J Phys Chem B 112(3):1007-1015.
    • (2008) J Phys Chem B , vol.112 , Issue.3 , pp. 1007-1015
    • Xiang, Y.1    Warshel, A.2
  • 31
    • 0035861065 scopus 로고    scopus 로고
    • Hydride transfer in liver alcohol dehydrogenase: Quantum dynamics, kinetic isotope effects, and role of enzyme motion
    • Billeter SR, Webb SP, Agarwal PK, Iordanov T, Hammes-Schiffer S (2001) Hydride transfer in liver alcohol dehydrogenase: Quantum dynamics, kinetic isotope effects, and role of enzyme motion. J Am Chem Soc 123(45):11262-11272.
    • (2001) J Am Chem Soc , vol.123 , Issue.45 , pp. 11262-11272
    • Billeter, S.R.1    Webb, S.P.2    Agarwal, P.K.3    Iordanov, T.4    Hammes-Schiffer, S.5
  • 32
    • 33748584863 scopus 로고    scopus 로고
    • Mechanisms and free energies of enzymatic reactions
    • Gao J, et al. (2006) Mechanisms and free energies of enzymatic reactions. Chem Rev 106(8):3188-3209.
    • (2006) Chem Rev , vol.106 , Issue.8 , pp. 3188-3209
    • Gao, J.1
  • 33
    • 84876156363 scopus 로고    scopus 로고
    • Direct simulation of proton-coupled electron transfer across multiple regimes
    • Kretchmer JS, Miller TF, 3rd (2013) Direct simulation of proton-coupled electron transfer across multiple regimes. J Chem Phys 138(13):134109.
    • (2013) J Chem Phys , vol.138 , Issue.13 , pp. 134109
    • Kretchmer, J.S.1    Miller III, T.F.2
  • 34
    • 34547245308 scopus 로고    scopus 로고
    • H and other transfers in enzymes and in solution: Theory and computations, a unified view Applications to experiment and computations
    • Marcus RA (2007) H and other transfers in enzymes and in solution: Theory and computations, a unified view. Applications to experiment and computations. J Phys Chem B 111(24):6643-6654
    • (2007) J Phys Chem B , vol.111 , Issue.24 , pp. 6643-6654
    • Marcus, R.A.1
  • 35
    • 0033305793 scopus 로고    scopus 로고
    • Proton and hydrogen atom tunneling in hydrolytic and redox enzyme catalysis
    • Kuznetsov AM, Ulstrup J (1999) Proton and hydrogen atom tunneling in hydrolytic and redox enzyme catalysis. Can J Chem 77(5-6):1085-1096.
    • (1999) Can J Chem , vol.77 , Issue.5-6 , pp. 1085-1096
    • Kuznetsov, A.M.1    Ulstrup, J.2
  • 36
    • 84873918133 scopus 로고    scopus 로고
    • Fluorescence of tryptophan in designed hairpin and Trpcage miniproteins: Measurements of fluorescence yields and calculations by quantum mechanical molecular dynamics simulations
    • McMillan AW, et al. (2013) Fluorescence of tryptophan in designed hairpin and Trpcage miniproteins: Measurements of fluorescence yields and calculations by quantum mechanical molecular dynamics simulations. J Phys Chem B 117(6):1790-1809.
    • (2013) J Phys Chem B , vol.117 , Issue.6 , pp. 1790-1809
    • McMillan, A.W.1
  • 37
    • 33749599714 scopus 로고    scopus 로고
    • Femtosecond studies of tryptophan fluorescence dynamics in proteins: Local solvation and electronic quenching
    • Zhang L, Kao YT, Qiu W, Wang L, Zhong D (2006) Femtosecond studies of tryptophan fluorescence dynamics in proteins: Local solvation and electronic quenching. J Phys Chem B 110(37):18097-18103.
    • (2006) J Phys Chem B , vol.110 , Issue.37 , pp. 18097-18103
    • Zhang, L.1    Kao, Y.T.2    Qiu, W.3    Wang, L.4    Zhong, D.5
  • 39
    • 72449122456 scopus 로고    scopus 로고
    • MOLCAS 7: The next generation
    • Aquilante F, et al. (2010) MOLCAS 7: The next generation. J Comput Chem 31(1): 224-247.
    • (2010) J Comput Chem , vol.31 , Issue.1 , pp. 224-247
    • Aquilante, F.1
  • 40
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus RA, Sutin N (1985) Electron transfers in chemistry and biology. Biochim Biophys Acta 811(3):265-322.
    • (1985) Biochim Biophys Acta , vol.811 , Issue.3 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 41
    • 78649627231 scopus 로고    scopus 로고
    • Predicting accurate electronic excitation transfer rates via Marcus theory with Boys or Edmiston-Ruedenberg localized diabatization
    • Subotnik JE, Vura-Weis J, Sodt AJ, Ratner MA (2010) Predicting accurate electronic excitation transfer rates via Marcus theory with Boys or Edmiston-Ruedenberg localized diabatization. J Phys Chem A 114(33):8665-8675.
    • (2010) J Phys Chem A , vol.114 , Issue.33 , pp. 8665-8675
    • Subotnik, J.E.1    Vura-Weis, J.2    Sodt, A.J.3    Ratner, M.A.4
  • 42
    • 79951801668 scopus 로고    scopus 로고
    • Triplet-triplet energy transfer in DNA: A process that occurs on the nanosecond timescale
    • Curutchet C, Voityuk AA (2011) Triplet-triplet energy transfer in DNA: A process that occurs on the nanosecond timescale. Angew Chem Int Ed Engl 50(8):1820-1822.
    • (2011) Angew Chem Int Ed Engl , vol.50 , Issue.8 , pp. 1820-1822
    • Curutchet, C.1    Voityuk, A.A.2
  • 43
    • 36749116146 scopus 로고
    • Monopole effects on electronic excitation interactions between large molecules Application to energy-transfer in chlorophylls
    • Chang JC (1977) Monopole effects on electronic excitation interactions between large molecules. Application to energy-transfer in chlorophylls. J Chem Phys 67(9): 3901-3909
    • (1977) J Chem Phys , vol.67 , Issue.9 , pp. 3901-3909
    • Chang, J.C.1
  • 44
    • 84874149006 scopus 로고    scopus 로고
    • A benchmark of excitonic couplings derived from atomic transition charges
    • Kistler KA, Spano FC, Matsika SA (2013) A benchmark of excitonic couplings derived from atomic transition charges. J Phys Chem B 117(7):2032-2044.
    • (2013) J Phys Chem B , vol.117 , Issue.7 , pp. 2032-2044
    • Kistler, K.A.1    Spano, F.C.2    Matsika, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.