메뉴 건너뛰기




Volumn 43, Issue 47, 2004, Pages 14881-14890

Light-induced structural changes of LOV domain-containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scattering

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; DIMERS; ENZYMES; MOLECULAR STRUCTURE; MUTAGENESIS; PIGMENTS; PLANTS (BOTANY); X RAY SCATTERING;

EID: 9744263917     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0485530     Document Type: Article
Times cited : (88)

References (44)
  • 1
    • 0036531885 scopus 로고    scopus 로고
    • Photosensory perception and signaling in plant cells: New paradigms?
    • Quail, P. H. (2002) Photosensory perception and signaling in plant cells: new paradigms? Curr. Opin. Cell Biol. 140, 180-188.
    • (2002) Curr. Opin. Cell Biol. , vol.140 , pp. 180-188
    • Quail, P.H.1
  • 2
    • 0036484368 scopus 로고    scopus 로고
    • Phytochrome photosensory signaling networks
    • Quail, P. H. (2002) Phytochrome photosensory signaling networks, Nat. Rev. Mol. Cell Biol. 3, 85-93.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 85-93
    • Quail, P.H.1
  • 3
    • 0141762747 scopus 로고    scopus 로고
    • Cryptochromes: Enabling plants and animals to determine circadian time
    • Cashmore, A. R. (2003) Cryptochromes: enabling plants and animals to determine circadian time, Cell 114, 537-543.
    • (2003) Cell , vol.114 , pp. 537-543
    • Cashmore, A.R.1
  • 5
    • 0036583102 scopus 로고    scopus 로고
    • Phototropins 1 and 2: Versatile plant blue-light receptors
    • Briggs, W. R., and Christie, J. M. (2002) Phototropins 1 and 2: versatile plant blue-light receptors, Trends Plant Sci. 7, 204-210.
    • (2002) Trends Plant Sci. , vol.7 , pp. 204-210
    • Briggs, W.R.1    Christie, J.M.2
  • 6
  • 7
    • 0035896393 scopus 로고    scopus 로고
    • Arabidopsis NPL1: A phototropin homolog controlling the chloroplast high-light avoidance response
    • Kagawa, T., Sakai, T., Suetsugu, N., Oikawa, K., Ishiguro, S., Kato, T., Tabata, S., Okada, K., and Wada, M. (2001) Arabidopsis NPL1: A phototropin homolog controlling the chloroplast high-light avoidance response, Science 291, 2138-2141.
    • (2001) Science , vol.291 , pp. 2138-2141
    • Kagawa, T.1    Sakai, T.2    Suetsugu, N.3    Oikawa, K.4    Ishiguro, S.5    Kato, T.6    Tabata, S.7    Okada, K.8    Wada, M.9
  • 8
    • 0035810965 scopus 로고    scopus 로고
    • Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii
    • Sakai, T., Kagawa, T., Kasahara, M., Swartz, T., Christie, J. M., Briggs, W. R., Wada, M., and Okada, K. (2001) Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii, Proc. Natl. Acad. Sci. U.S.A. 98, 6969-6974.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6969-6974
    • Sakai, T.1    Kagawa, T.2    Kasahara, M.3    Swartz, T.4    Christie, J.M.5    Briggs, W.R.6    Wada, M.7    Okada, K.8
  • 9
    • 0035912211 scopus 로고    scopus 로고
    • Phototropin-related NPL1 controls chloroplast relocation induced by blue light
    • Jarillo, G. A., Gabrys, H., Capel, J., Alonso, J. M., Ecker, J. R., and Cashmore, A. R. (2001) Phototropin-related NPL1 controls chloroplast relocation induced by blue light, Nature 410, 952-954.
    • (2001) Nature , vol.410 , pp. 952-954
    • Jarillo, G.A.1    Gabrys, H.2    Capel, J.3    Alonso, J.M.4    Ecker, J.R.5    Cashmore, A.R.6
  • 10
    • 0035818967 scopus 로고    scopus 로고
    • Phot1 and phot2 mediate blue light regulation of stomatal opening
    • Kinoshita, T., Doi, M., Suetsugu, N., Kagawa, T., Wada, M., and Shimazaki, K. (2001) Phot1 and phot2 mediate blue light regulation of stomatal opening, Nature 414, 656-660.
    • (2001) Nature , vol.414 , pp. 656-660
    • Kinoshita, T.1    Doi, M.2    Suetsugu, N.3    Kagawa, T.4    Wada, M.5    Shimazaki, K.6
  • 11
    • 0029278701 scopus 로고
    • Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli
    • Liscum, E., and Briggs, W. R. (1995) Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli, Plant Cell 7, 473-485.
    • (1995) Plant Cell , vol.7 , pp. 473-485
    • Liscum, E.1    Briggs, W.R.2
  • 12
    • 0034985095 scopus 로고    scopus 로고
    • The enhancement of phototropin-induced phototropic curvature in Arabidopsis occurs via a photoreversible phytochrome A-dependent modulation of auxin responsiveness
    • Stowe-Evans, E. L., Luesse, D. R., and Liscum, E. (2002) The enhancement of phototropin-induced phototropic curvature in Arabidopsis occurs via a photoreversible phytochrome A-dependent modulation of auxin responsiveness, Plant Physiol. 2001, 826-834.
    • (2002) Plant Physiol. , vol.2001 , pp. 826-834
    • Stowe-Evans, E.L.1    Luesse, D.R.2    Liscum, E.3
  • 15
    • 0033570171 scopus 로고    scopus 로고
    • (+)-ATPase by phosphorylation of the C-terminus in stomatal guard cells
    • (+)-ATPase by phosphorylation of the C-terminus in stomatal guard cells, EMBO J. 18, 5548-5558.
    • (1999) EMBO J. , vol.18 , pp. 5548-5558
    • Kinoshita, T.1    Shimazaki, K.2
  • 16
    • 0033587744 scopus 로고    scopus 로고
    • LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): Binding sites for the chromophore flavin mononucleotide
    • Christie, J. M., Salomon, M., Nozue, K., Wada, M., and Briggs, W. R. (1999) LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide, Proc. Natl. Acad. Sci. U.S.A. 96, 8779-8783.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8779-8783
    • Christie, J.M.1    Salomon, M.2    Nozue, K.3    Wada, M.4    Briggs, W.R.5
  • 17
    • 0038623933 scopus 로고    scopus 로고
    • Functional conservation of light, oxygen, or voltage domains in light sensing
    • Cheng, P., He, Q., Yang, Y., Wang, L., and Liu, Y. (2003) Functional conservation of light, oxygen, or voltage domains in light sensing, Proc. Natl. Acad. Sci. U.S.A. 100, 5938-5943.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5938-5943
    • Cheng, P.1    He, Q.2    Yang, Y.3    Wang, L.4    Liu, Y.5
  • 18
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential and light
    • Taylor, B. L., and Zhulin, I. B. (1999) PAS domains: internal sensors of oxygen, redox potential and light, Microbiol. Mol. Biol. Rev. 63, 479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 19
    • 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, S. M., Massy, V., Ballou, D., Williams, C. H., Jr., Distefano, M. D., Moore, M. J., and Walsh, C. T. (1990) 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.
    • (1990) Biochemistry , vol.29 , pp. 2831-2841
    • Miller, S.M.1    Massy, V.2    Ballou, D.3    Williams Jr., C.H.4    Distefano, M.D.5    Moore, M.J.6    Walsh, C.T.7
  • 20
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • Salomon, M., Christie, J. M., Kneib, E., Lempert, U., and Briggs, W. R. (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    Kneib, E.3    Lempert, U.4    Briggs, W.R.5
  • 22
    • 0037048688 scopus 로고    scopus 로고
    • Photoreaction of the cysteine S-H group in the LOV2 domain of Adiantum phytochrome3
    • Iwata, T., Tokutomi, S., and Kandori, H. (2002) Photoreaction of the cysteine S-H group in the LOV2 domain of Adiantum phytochrome3, J. Am. Chem. Soc. 124, 11840-11841.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11840-11841
    • Iwata, T.1    Tokutomi, S.2    Kandori, H.3
  • 23
    • 0037489440 scopus 로고    scopus 로고
    • Light-induced structural changes in the LOV2 domain of Adiantum phytochrome3 studied by low-temperature FTIR and UV-visible spectroscopy
    • Iwata, T., Nozaki, D., Tokutomi, S., Kagawa, T., Wada, M., and Kandori, H. (2003) Light-induced structural changes in the LOV2 domain of Adiantum phytochrome3 studied by low-temperature FTIR and UV-visible spectroscopy, Biochemistry 42, 8183-8191.
    • (2003) Biochemistry , vol.42 , pp. 8183-8191
    • Iwata, T.1    Nozaki, D.2    Tokutomi, S.3    Kagawa, T.4    Wada, M.5    Kandori, H.6
  • 24
    • 0037380836 scopus 로고    scopus 로고
    • Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii
    • Fedorov, R., Schlichting, I., Hartmann, E., Domratcheva, T., Fuhrmann, M., and Hegemann, P. (2003) Crystal structures and molecular mechanism of a light-induced signaling switch: The Phot-LOV1 domain from Chlamydomonas reinhardtii, Biophys. J. 84, 2474-2482.
    • (2003) Biophys. J. , vol.84 , pp. 2474-2482
    • Fedorov, R.1    Schlichting, I.2    Hartmann, E.3    Domratcheva, T.4    Fuhrmann, M.5    Hegemann, P.6
  • 25
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into ligand-mediated signal transduction
    • Crosson, S., and Moffat, K. (2001) Structure of a flavin-binding plant photoreceptor domain: Insights into ligand-mediated signal transduction, Proc. Natl. Acad. Sci. U.S.A. 98, 2995-3000.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 26
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson, S., and 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
  • 27
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • Crosson, S., Rajagopal, S., and Moffat, K. (2003) The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains, Biochemistry 42, 2-10.
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 28
    • 0036776294 scopus 로고    scopus 로고
    • Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function
    • Christie, J. M., Swartz, T. E., Bogomolni, R. A., and Briggs, W. R. (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.A.3    Briggs, W.R.4
  • 29
    • 0141707094 scopus 로고    scopus 로고
    • Structural basis of a phototropin light switch
    • Harper, S. M., Neil, L. C., and Gardner, K. H. (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
  • 31
    • 0033433484 scopus 로고    scopus 로고
    • The use of a Hamamatsu X-ray image intensifier with a cooled CCD as a solution X-ray scattering detector
    • Fujisawa, T., Inoko, Y., and Yagi, N. (1999) The use of a Hamamatsu X-ray image intensifier with a cooled CCD as a solution X-ray scattering detector, J. Synchrotron Radiat. 6, 1106-1114.
    • (1999) J. Synchrotron Radiat. , vol.6 , pp. 1106-1114
    • Fujisawa, T.1    Inoko, Y.2    Yagi, N.3
  • 33
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria, J. Appl. Crystallogr. 25, 495-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 34
    • 0346457106 scopus 로고    scopus 로고
    • Conformational variability of nucleo-cytoplasmic transport factor
    • Fukuhara, N., Fernandez, E., Ebert, J., Conti, E., and Svergun, D. (2004) Conformational variability of nucleo-cytoplasmic transport factor, J. Biol. Chem. 279, 2176-2181.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2176-2181
    • Fukuhara, N.1    Fernandez, E.2    Ebert, J.3    Conti, E.4    Svergun, D.5
  • 35
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun, D. I. (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing, Biophys. J. 76, 2879-2886.
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 36
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V., and Koch, M. H. J. (2001) Determination of domain structure of proteins from X-ray solution scattering, Biophys. J. 80, 2946-2953.
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 37
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin, M. B., and Svergun, D. I. (2001) Automated matching of high- and low-resolution structural models, J. Appl. Crystallogr. 34, 33-41.
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 39
    • 4143081643 scopus 로고    scopus 로고
    • Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV domain
    • Salomon, M., Lempert, U., and Rüdiger, W. (2004) Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV domain, FEBS Lett. 572, 8-10.
    • (2004) FEBS Lett. , vol.572 , pp. 8-10
    • Salomon, M.1    Lempert, U.2    Rüdiger, W.3
  • 40
    • 0029017976 scopus 로고
    • Protein-protein interaction via PAS domains: Role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt
    • Lindebro, M. C., Poellinger, L., and Whitelaw, M. L. (1995) Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt, EMBO J. 14, 3528-3539.
    • (1995) EMBO J. , vol.14 , pp. 3528-3539
    • Lindebro, M.C.1    Poellinger, L.2    Whitelaw, M.L.3
  • 42
    • 0031880316 scopus 로고    scopus 로고
    • Roles in dimerization and blue light photoresponse of the PAS and LOV domains of Neurospora crassa white collar proteins
    • Ballario, P., Talora, C., Galli, D., Linden, H., and Macino, G. (1998) Roles in dimerization and blue light photoresponse of the PAS and LOV domains of Neurospora crassa white collar proteins, Mol. Microbiol. 29, 719-729.
    • (1998) Mol. Microbiol. , vol.29 , pp. 719-729
    • Ballario, P.1    Talora, C.2    Galli, D.3    Linden, H.4    Macino, G.5
  • 43
    • 0036774056 scopus 로고    scopus 로고
    • Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation
    • Amezcua, A. A., Harper, S. M., Rutter, J., and Gardner, K. H. (2002) Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation, Structure 10, 1349-1361.
    • (2002) Structure , vol.10 , pp. 1349-1361
    • Amezcua, A.A.1    Harper, S.M.2    Rutter, J.3    Gardner, K.H.4
  • 44
    • 0000107715 scopus 로고    scopus 로고
    • ASSA: A program for three-dimensional rendering in solution scattering from biopolymers
    • Kozin, M. B., and Svergun, D. I. (1997) ASSA: A program for three-dimensional rendering in solution scattering from biopolymers, J. Appl. Crystallogr. 34, 33-41.
    • (1997) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.