메뉴 건너뛰기




Volumn 1, Issue , 2015, Pages

Dynamic crystallography reveals early signalling events in ultraviolet photoreceptor UVR8

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84988044679     PISSN: 2055026X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nplants.2014.6     Document Type: Article
Times cited : (45)

References (36)
  • 1
    • 84859646883 scopus 로고    scopus 로고
    • UV-B photoreceptor-mediated signalling in plants
    • Heijde, M. & Ulm, R. UV-B photoreceptor-mediated signalling in plants. Trends Plant Sci. 17, 230-237 (2012).
    • (2012) Trends Plant Sci , vol.17 , pp. 230-237
    • Heijde, M.1    Ulm, R.2
  • 2
    • 79959747572 scopus 로고    scopus 로고
    • Functional interaction of the circadian clock and UV RESISTANCE LOCUS 8-controlled UV-B signaling pathways in Arabidopsis thaliana
    • Fehér, B. et al. Functional interaction of the circadian clock and UV RESISTANCE LOCUS 8-controlled UV-B signaling pathways in Arabidopsis thaliana. Plant J. 67, 37-48 (2011).
    • (2011) Plant J , vol.67 , pp. 37-48
    • Fehér, B.1
  • 3
    • 77954961929 scopus 로고    scopus 로고
    • Ultraviolet stress delays chromosome replication in light/dark synchronized cells of the marine cyanobacterium Prochlorococcus marinus PCC9511
    • Kolowrat, C. et al. Ultraviolet stress delays chromosome replication in light/dark synchronized cells of the marine cyanobacterium Prochlorococcus marinus PCC9511. BMC Microbiol. 10, 204 (2010).
    • (2010) BMC Microbiol , vol.10 , pp. 204
    • Kolowrat, C.1
  • 4
    • 84896858372 scopus 로고    scopus 로고
    • The UV-B photoreceptor UVR8: From structure to physiology
    • Jenkins, G. I. The UV-B photoreceptor UVR8: from structure to physiology. Plant Cell 26, 21-37 (2014).
    • (2014) Plant Cell , vol.26 , pp. 21-37
    • Jenkins, G.I.1
  • 5
    • 0002893929 scopus 로고
    • Plants and near-ultraviolet radiation
    • Klein, R. M. Plants and near-ultraviolet radiation. Bot. Rev. 44, 1-127 (1978).
    • (1978) Bot. Rev , vol.44 , pp. 1-127
    • Klein R. ., M.1
  • 6
    • 79953272725 scopus 로고    scopus 로고
    • Perception of UV-B by the arabidopsis UVR8 protein
    • Rizzini, L. et al. Perception of UV-B by the Arabidopsis UVR8 Protein. Science 332, 103-106 (2011).
    • (2011) Science , vol.332 , pp. 103-106
    • Rizzini, L.1
  • 7
    • 62049085316 scopus 로고    scopus 로고
    • Interaction of COP1 and UVR8 regulates UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis
    • Favory, J.-J. et al. Interaction of COP1 and UVR8 regulates UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis. EMBO J. 28, 591-601 (2009).
    • (2009) EMBO J , vol.28 , pp. 591-601
    • Favory, J.-J.1
  • 8
    • 29144433413 scopus 로고    scopus 로고
    • A UV-B-specific signaling component orchestrates plant UV protection
    • Brown, B. A. et al. A UV-B-specific signaling component orchestrates plant UV protection. Proc. Natl Acad. Sci. USA 102, 18225-18230 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18225-18230
    • Brown, B.A.1
  • 9
    • 84862776742 scopus 로고    scopus 로고
    • Structural basis of ultraviolet-B perception by UVR8
    • Wu, D. et al. Structural basis of ultraviolet-B perception by UVR8. Nature 484, 214-219 (2012).
    • (2012) Nature , vol.484 , pp. 214-219
    • Wu, D.1
  • 10
    • 84863393216 scopus 로고    scopus 로고
    • Plant UVR8 photoreceptor senses UV-B by tryptophanmediated disruption of cross-dimer salt bridges
    • Christie, J. M. et al. Plant UVR8 photoreceptor senses UV-B by tryptophanmediated disruption of cross-dimer salt bridges. Science 335, 1492-1496 (2012).
    • (2012) Science , vol.335 , pp. 1492-1496
    • Christie, J.M.1
  • 11
    • 84868159269 scopus 로고    scopus 로고
    • In vivo function of tryptophans in the Arabidopsis UV-B photoreceptor UVR8
    • O'Hara, A. & Jenkins, G. I. In vivo function of tryptophans in the Arabidopsis UV-B photoreceptor UVR8. Plant Cell 24, 3755-3766 (2012).
    • (2012) Plant Cell , vol.24 , pp. 3755-3766
    • O'Hara, A.1    Jenkins, G.I.2
  • 12
    • 84880534992 scopus 로고    scopus 로고
    • Interactions and stabilities of the UV RESISTANCE LOCUS8 (UVR8) protein dimer and its key mutants
    • Wu, M., Strid, Å. & Eriksson, L. A. Interactions and stabilities of the UV RESISTANCE LOCUS8 (UVR8) protein dimer and its key mutants. J. Chem. Inf. Model. 53, 1736-1746 (2013).
    • (2013) J. Chem. Inf. Model , vol.53 , pp. 1736-1746
    • Wu, M.1    Strid, A.2    Eriksson, L.A.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. C-terminal region of the UV-B photoreceptor UVR8 initiates signaling through interaction with the COP1 protein. Proc. Natl Acad. Sci. USA 109, 16366-16370 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 16366-16370
    • Cloix, C.1
  • 14
    • 0036742711 scopus 로고    scopus 로고
    • Arabidopsis UVR8 regulates ultraviolet-B signal transduction and tolerance and contains sequence similarity to human regulator of chromatin condensation 1
    • Kliebenstein, D. J., Lim, J. E., Landry, L. G. & Last, R. L. Arabidopsis UVR8 regulates ultraviolet-B signal transduction and tolerance and contains sequence similarity to human regulator of chromatin condensation 1. Plant Physiol. 130, 234-243 (2002).
    • (2002) Plant Physiol , vol.130 , pp. 234-243
    • Kliebenstein, D.J.1    Lim, J.E.2    Landry, L.G.3    Last, R.L.4
  • 15
    • 84868095939 scopus 로고    scopus 로고
    • The molecular mechanism of the UVR8 UV-B photoreceptor
    • Hofmann, N. R. The molecular mechanism of the UVR8 UV-B photoreceptor. Plant Cell 24, 3485-3485 (2012).
    • (2012) Plant Cell , vol.24 , pp. 3485-3485
    • Hofmann, N.R.1
  • 16
    • 84893504425 scopus 로고    scopus 로고
    • Photochemical reaction mechanism of UV-B-induced monomerization of UVR8 dimers as the first signaling event in UV-B-regulated gene expression in plants
    • Wu, M., Strid, Å. & Eriksson, L. A. Photochemical reaction mechanism of UV-B-induced monomerization of UVR8 dimers as the first signaling event in UV-B-regulated gene expression in plants. J. Phys. Chem. B 118, 951-965 (2014).
    • (2014) J. Phys. Chem. B , vol.118 , pp. 951-965
    • Wu, M.1    Strid, A.2    Eriksson, L.A.3
  • 17
    • 84992111030 scopus 로고    scopus 로고
    • On the mechanism of photoinduced dimer dissociation in the plant UVR8 photoreceptor
    • Voityuk, A. A., Marcus, R. A. & Michel-Beyerle, M.-E. On the mechanism of photoinduced dimer dissociation in the plant UVR8 photoreceptor. Proc. Natl Acad. Sci. USA 111, 5219-5224 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 5219-5224
    • Voityuk, A.A.1    Marcus, R.A.2    Michel-Beyerle, M.-E.3
  • 18
    • 84891753192 scopus 로고    scopus 로고
    • Quenching dynamics of ultraviolet-light perception by UVR8 photoreceptor
    • Liu, Z. et al. Quenching dynamics of ultraviolet-light perception by UVR8 photoreceptor. J. Phys. Chem. Lett. 5, 69-72 (2014).
    • (2014) J. Phys. Chem. Lett , vol.5 , pp. 69-72
    • Liu, Z.1
  • 19
    • 81555214075 scopus 로고    scopus 로고
    • Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome
    • Yang, X., Ren, Z., Kuk, J. & Moffat, K. Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome. Nature 479, 428-432 (2011).
    • (2011) Nature , vol.479 , pp. 428-432
    • Yang, X.1    Ren, Z.2    Kuk, J.3    Moffat, K.4
  • 20
    • 0035923399 scopus 로고    scopus 로고
    • A molecular movie at 1.8 Å resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds
    • Ren, Z. et al. A molecular movie at 1.8 Å resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds. Biochemistry (Mosc.) 40, 13788-13801 (2001).
    • (2001) Biochemistry (Mosc.) , vol.40 , pp. 13788-13801
    • Ren, Z.1
  • 21
    • 84878270702 scopus 로고    scopus 로고
    • Resolution of structural heterogeneity in dynamic crystallography
    • Ren, Z. et al. Resolution of structural heterogeneity in dynamic crystallography. Acta Crystallogr. Sect. D 69, 946-959 (2013).
    • (2013) Acta Crystallogr. Sect D , vol.69 , pp. 946-959
    • Ren, Z.1
  • 22
    • 84897452651 scopus 로고    scopus 로고
    • Photoactivated UVR8- COP1 Module determines photomorphogenic UV-B signaling output in Arabidopsis
    • Huang, X., Yang, P., Ouyang, X., Chen, L. & Deng, X.W. Photoactivated UVR8- COP1 Module determines photomorphogenic UV-B signaling output in Arabidopsis. PLoS Genet. 10, e1004218 (2014).
    • (2014) PLoS Genet , vol.10 , pp. e1004218
    • Huang, X.1    Yang, P.2    Ouyang, X.3    Chen, L.4    Deng, X.W.5
  • 23
    • 84922643902 scopus 로고    scopus 로고
    • Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy
    • Heilmann, M., Christie, J. M., Kennis, J. T. M., Jenkins, G. I. & Mathes, T. Photoinduced transformation of UVR8 monitored by vibrational and fluorescence spectroscopy. Photochem. Photobiol. Sci. http://dx.doi.org/10.1039/C4PP00246F (2014).
    • (2014) Photochem. Photobiol. Sci
    • Heilmann, M.1    Christie, J.M.2    Kennis, J.T.M.3    Jenkins, G.I.4    Mathes, T.5
  • 24
    • 22144458712 scopus 로고    scopus 로고
    • Selective excitation of tryptophan fluorescence decay in proteins using a subnanosecond 295 nm light-emitting diode and time-correlated single-photon counting
    • McGuinness, C. D., Sagoo, K., McLoskey, D. & Birch, D. J. S. Selective excitation of tryptophan fluorescence decay in proteins using a subnanosecond 295 nm light-emitting diode and time-correlated single-photon counting. Appl. Phys. Lett. 86, 261911 (2005).
    • (2005) Appl. Phys. Lett , vol.86 , pp. 261911
    • McGuinness, C.D.1    Sagoo, K.2    McLoskey, D.3    Birch, D.J.S.4
  • 25
    • 4544285943 scopus 로고    scopus 로고
    • Ultraviolet light-emitting diodes operating in the 340 nm wavelength range and application to time-resolved fluorescence spectroscopy
    • Peng, H. et al. Ultraviolet light-emitting diodes operating in the 340 nm wavelength range and application to time-resolved fluorescence spectroscopy. Appl. Phys. Lett. 85, 1436-1438 (2004).
    • (2004) Appl. Phys. Lett , vol.85 , pp. 1436-1438
    • Peng, H.1
  • 26
    • 84890282620 scopus 로고    scopus 로고
    • Constitutively active UVR8 photoreceptor variant in Arabidopsis
    • Heijde, M. et al. Constitutively active UVR8 photoreceptor variant in Arabidopsis. Proc. Natl Acad. Sci. USA 110, 20326-20331 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 20326-20331
    • Heijde, M.1
  • 27
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E. J., Schmidt, C. J., Nambudripad, R. & Smith, T. F. The ancient regulatory-protein family of WD-repeat proteins. Nature 371, 297-300 (1994).
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 28
    • 0024961673 scopus 로고
    • Light guides. Directional energy transfer in a photosynthetic antenna
    • Glazer, A. N. Light guides. Directional energy transfer in a photosynthetic antenna. J. Biol. Chem. 264, 1-4 (1989).
    • (1989) J. Biol. Chem , vol.264 , pp. 1-4
    • Glazer, A.N.1
  • 29
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution
    • Liu, Z. et al. Crystal structure of spinach major light-harvesting complex at 2.72 Å resolution. Nature 428, 287-292 (2004).
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1
  • 30
    • 0001257583 scopus 로고
    • Construction of tight-binding-like potentials on the basis of density-functional theory: Application to carbon
    • Porezag, D., Frauenheim, T., Köhler, T., Seifert, G. & Kaschner, R. Construction of tight-binding-like potentials on the basis of density-functional theory: Application to carbon. Phys. Rev. B 51, 12947-12957 (1995).
    • (1995) Phys. Rev B , vol.51 , pp. 12947-12957
    • Porezag, D.1    Frauenheim, T.2    Köhler, T.3    Seifert, G.4    Kaschner, R.5
  • 31
    • 1542779956 scopus 로고    scopus 로고
    • Self-consistent-charge density-functional tight-binding method for simulations of complex materials properties
    • Elstner, M. et al. Self-consistent-charge density-functional tight-binding method for simulations of complex materials properties. Phys. Rev. B 58, 7260-7268 (1998).
    • (1998) Phys. Rev B , vol.58 , pp. 7260-7268
    • Elstner, M.1
  • 32
    • 4243706463 scopus 로고    scopus 로고
    • Tight-binding approach to time-dependent densityfunctional response theory
    • Niehaus, T. A. et al. Tight-binding approach to time-dependent densityfunctional response theory. Phys. Rev. B 63, 085108 (2001).
    • (2001) Phys. Rev B , vol.63 , pp. 085108
    • Niehaus, T.A.1
  • 33
    • 70349750169 scopus 로고    scopus 로고
    • Approximate time-dependent density functional theory
    • Niehaus, T. A. Approximate time-dependent density functional theory. J. Mol. Struct. THEOCHEM 914, 38-49 (2009).
    • (2009) J. Mol. Struct. THEOCHEM , vol.914 , pp. 38-49
    • Niehaus, T.A.1
  • 34
    • 29544448844 scopus 로고    scopus 로고
    • Modeling the absorption spectrum of tryptophan in proteins
    • Rogers, D. M., Besley, N. A., O'Shea, P. & Hirst, J. D. Modeling the absorption spectrum of tryptophan in proteins. J. Phys. Chem. B 109, 23061-23069 (2005).
    • (2005) J. Phys. Chem B , vol.109 , pp. 23061-23069
    • Rogers, D.M.1    Besley, N.A.2    O'Shea, P.3    Hirst, J.D.4
  • 35
    • 0034877118 scopus 로고    scopus 로고
    • Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues
    • Reshetnyak, Y. K., Koshevnik, Y. & Burstein, E. A. Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues. Biophys. J. 81, 1735-1758 (2001).
    • (2001) Biophys. J , vol.81 , pp. 1735-1758
    • Reshetnyak, Y.K.1    Koshevnik, Y.2    Burstein, E.A.3
  • 36
    • 77951854791 scopus 로고    scopus 로고
    • Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction
    • Wöhri, A. B. et al. Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction. Science 328, 630-633 (2010).
    • (2010) Science , vol.328 , pp. 630-633
    • Wöhri, A.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.