메뉴 건너뛰기




Volumn 91, Issue 10, 2006, Pages 3797-3804

Time-resolved detection of conformational changes in oat phytochrome A: Time-dependent diffusion

Author keywords

[No Author keywords available]

Indexed keywords

PHYTOCHROME; PHYTOCHROME A; UNCLASSIFIED DRUG;

EID: 33751216180     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.092882     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 0000797127 scopus 로고
    • Phytochrome: Chemical and physical properties and mechanism of action
    • Briggs, W. R., and H. V. Rice. 1972. Phytochrome: chemical and physical properties and mechanism of action. Annu. Rev. Plant Physiol. 23:293-334.
    • (1972) Annu. Rev. Plant Physiol. , vol.23 , pp. 293-334
    • Briggs, W.R.1    Rice, H.V.2
  • 3
    • 0028936558 scopus 로고
    • Photobiophysics and photobiochemistry of the heterogeneous phytochrome system
    • Sineshchekov, V. A. 1995. Photobiophysics and photobiochemistry of the heterogeneous phytochrome system. Biochim. Biophys. Acta. 1228:125-164.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 125-164
    • Sineshchekov, V.A.1
  • 4
    • 0024050150 scopus 로고
    • The molecular topography of phytochrome: Chromophore and apoprotein
    • Song, P.-S. 1988. The molecular topography of phytochrome: chromophore and apoprotein. J. Photochem. Photobiol. B. 2:43-57.
    • (1988) J. Photochem. Photobiol. B , vol.2 , pp. 43-57
    • Song, P.-S.1
  • 5
    • 0030087691 scopus 로고    scopus 로고
    • The amino-terminus of phytochrome A contains two distinct functional domains
    • Jordan, E. T., J. R. Cherry, J. M. Walker, and R. D. Viestra. 1996. The amino-terminus of phytochrome A contains two distinct functional domains. Plant J. 9:243-257.
    • (1996) Plant J. , vol.9 , pp. 243-257
    • Jordan, E.T.1    Cherry, J.R.2    Walker, J.M.3    Viestra, R.D.4
  • 6
    • 0042068123 scopus 로고    scopus 로고
    • Dimers of the N-terminal domain of phytochrome B are functional in the nucleus
    • Matsushita, T., N. Mochizuki, and A. Nagatani. 2003. Dimers of the N-terminal domain of phytochrome B are functional in the nucleus. Nature. 424:571-574.
    • (2003) Nature , vol.424 , pp. 571-574
    • Matsushita, T.1    Mochizuki, N.2    Nagatani, A.3
  • 7
    • 0038368428 scopus 로고
    • Tertiary structure of phytochrome probed by quasi-elastic light scattering and rotational relaxation time measurements
    • Sarkar, H. K., D. K. Moon, P.-S. Song, T. Chang, and H. Yu. 1984. Tertiary structure of phytochrome probed by quasi-elastic light scattering and rotational relaxation time measurements. Biochemistry. 23: 1882-1888.
    • (1984) Biochemistry , vol.23 , pp. 1882-1888
    • Sarkar, H.K.1    Moon, D.K.2    Song, P.-S.3    Chang, T.4    Yu, H.5
  • 8
    • 0024652229 scopus 로고
    • Domain structure of 124-kiloDalton phytochrome from Avena sativa visualized by electron micrography
    • Jones, A. M., and H. P. Erickson. 1989. Domain structure of 124-kiloDalton phytochrome from Avena sativa visualized by electron micrography. Photochem. Photobiol. 49:479-483.
    • (1989) Photochem. Photobiol. , vol.49 , pp. 479-483
    • Jones, A.M.1    Erickson, H.P.2
  • 10
    • 84987034464 scopus 로고
    • Quaternary structure of pea phytochrome I dimer studied with small-angle x-ray scattering and rotary-shadowing electron microscopy
    • Nakasako, M., M. Wada, S. Tokutomi, K. T. Yamamoto, J. Sakai, M. Kataoka, F. Tokunaga, and M. Furuya. 1990. Quaternary structure of pea phytochrome I dimer studied with small-angle x-ray scattering and rotary-shadowing electron microscopy. Photochem. Photobiol. 52:3-12.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 3-12
    • Nakasako, M.1    Wada, M.2    Tokutomi, S.3    Yamamoto, K.T.4    Sakai, J.5    Kataoka, M.6    Tokunaga, F.7    Furuya, M.8
  • 11
    • 0022431885 scopus 로고
    • Structure function studies on phytochrome
    • Lagarias, J. C., and F. M. Mercurio. 1985. Structure function studies on phytochrome. J. Biol. Chem. 260:2415-2423.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2415-2423
    • Lagarias, J.C.1    Mercurio, F.M.2
  • 12
    • 0019883188 scopus 로고
    • Physicochemical difference between the red- and the far-red-absorbing forms of phytochrome
    • Hunt, R. E., and L. H. Pratt. 1981. Physicochemical difference between the red- and the far-red-absorbing forms of phytochrome. Biochemistry. 20:941-945.
    • (1981) Biochemistry , vol.20 , pp. 941-945
    • Hunt, R.E.1    Pratt, L.H.2
  • 13
    • 0028264231 scopus 로고
    • Phototransformation of pea phytochrome A induces an increase in α-helical folding of the apoprotein: Comparison with a Monocot phytochrome A and CD analysis by different methods
    • Deforce, L., S. Tokutomi, and P.-S. Song. 1994. Phototransformation of pea phytochrome A induces an increase in α-helical folding of the apoprotein: comparison with a Monocot phytochrome A and CD analysis by different methods. Biochemistry. 33:4918-4922.
    • (1994) Biochemistry , vol.33 , pp. 4918-4922
    • Deforce, L.1    Tokutomi, S.2    Song, P.-S.3
  • 14
    • 0023651195 scopus 로고
    • A photoreversible circular dichroism spectral change in oat phytochrome is suppressed by a monoclonal antibody that binds near its N-terminus and by chromophore modification
    • Chai, Y. G., P.-S. Song, M. M. Cordonnier, and L. H. Pratt. 1987. A photoreversible circular dichroism spectral change in oat phytochrome is suppressed by a monoclonal antibody that binds near its N-terminus and by chromophore modification. Biochemistry. 26:4947-4952.
    • (1987) Biochemistry , vol.26 , pp. 4947-4952
    • Chai, Y.G.1    Song, P.-S.2    Cordonnier, M.M.3    Pratt, L.H.4
  • 15
    • 0013544056 scopus 로고
    • Small-angle x-ray scattering studies on the macromolecular structure of the red-light-absorbing form of 121 kDa pea phytochrome and its 114 kDa chromopeptide
    • Tokutomi, S., M. Kataoka, J. Sakai, M. Nakasako, F. Tokunaga, M. Tasumi, and M. Furuya. 1988. Small-angle x-ray scattering studies on the macromolecular structure of the red-light-absorbing form of 121 kDa pea phytochrome and its 114 kDa chromopeptide. Biochim. Biophys. Acta. 953:297-305.
    • (1988) Biochim. Biophys. Acta , vol.953 , pp. 297-305
    • Tokutomi, S.1    Kataoka, M.2    Sakai, J.3    Nakasako, M.4    Tokunaga, F.5    Tasumi, M.6    Furuya, M.7
  • 16
    • 12544260512 scopus 로고    scopus 로고
    • Light-induced global structural changes in phytochrome A regulating photomorphogenesis in plants
    • Nakasako, M., T. Iwata, K. Inoue, and S. Tokutomi. 2005. Light-induced global structural changes in phytochrome A regulating photomorphogenesis in plants. FEBS J. 272:603-612.
    • (2005) FEBS J. , vol.272 , pp. 603-612
    • Nakasako, M.1    Iwata, T.2    Inoue, K.3    Tokutomi, S.4
  • 17
    • 84989674032 scopus 로고
    • Evidence for a sequential pathway from Pr to Pfr of the phototransformation of 124-kDa oat phytochrome
    • Eilfeld, P., P. Eilfeld, J. Vogel, and R. Maurer. 1987. Evidence for a sequential pathway from Pr to Pfr of the phototransformation of 124-kDa oat phytochrome. Photochem. Photobiol. 45:825-830.
    • (1987) Photochem. Photobiol. , vol.45 , pp. 825-830
    • Eilfeld, P.1    Eilfeld, P.2    Vogel, J.3    Maurer, R.4
  • 19
    • 0038301978 scopus 로고    scopus 로고
    • The time-resolved thermodynamics of the chromophore-protein interactions in biological photosensors as derived from photothermal measurements
    • Losi, A., and S. E. Braslavsky. 2003. The time-resolved thermodynamics of the chromophore-protein interactions in biological photosensors as derived from photothermal measurements. Phys. Chem. Chem. Phys. 5:2739-2750.
    • (2003) Phys. Chem. Chem. Phys. , vol.5 , pp. 2739-2750
    • Losi, A.1    Braslavsky, S.E.2
  • 20
    • 0001010727 scopus 로고
    • Time-resolved UV circular dichroism of phytochrome A: Folding of the N-terminal region
    • Chen, E. F., W. Parker, J. W. Lewis, P.-S. Song, and D. S. Kliger. 1993. Time-resolved UV circular dichroism of phytochrome A: folding of the N-terminal region. J. Am. Chem. Soc. 115:9854-9855.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9854-9855
    • Chen, E.F.1    Parker, W.2    Lewis, J.W.3    Song, P.-S.4    Kliger, D.S.5
  • 21
    • 0030991773 scopus 로고    scopus 로고
    • Dynamics of the N-terminal α-helix unfolding in the photoreversion reaction of phytochrome A
    • Chen, E. F., V. N. Lapko, P.-S. Song, and D. S. Kliger. 1997. Dynamics of the N-terminal α-helix unfolding in the photoreversion reaction of phytochrome A. Biochemistry. 36:4903-4908.
    • (1997) Biochemistry , vol.36 , pp. 4903-4908
    • Chen, E.F.1    Lapko, V.N.2    Song, P.-S.3    Kliger, D.S.4
  • 24
    • 16644381874 scopus 로고    scopus 로고
    • Kinetics of intermolecular interaction during protein folding of reduced cytochrome c
    • Nishida, S., T. Nada, and M. Terazima. 2004. Kinetics of intermolecular interaction during protein folding of reduced cytochrome c. Biophys. J. 87:2663-2675.
    • (2004) Biophys. J. , vol.87 , pp. 2663-2675
    • Nishida, S.1    Nada, T.2    Terazima, M.3
  • 25
    • 25444492902 scopus 로고    scopus 로고
    • Conformational dynamics of phototropin 2 LOV2 domain with the linker upon photoexcitation
    • Eitoku, T., Y. Nakasone, D. Matsuoka, S. Tokutomi, and M. Terazima. 2005. Conformational dynamics of phototropin 2 LOV2 domain with the linker upon photoexcitation. J. Am. Chem. Soc. 127:13238-13244.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13238-13244
    • Eitoku, T.1    Nakasone, Y.2    Matsuoka, D.3    Tokutomi, S.4    Terazima, M.5
  • 26
    • 0001636568 scopus 로고
    • Translational diffusion of a transient radical studied by the transient grating method, pyrazinyl radical in 2-propanol
    • Terazima, M., and N. Hirota. 1993. Translational diffusion of a transient radical studied by the transient grating method, pyrazinyl radical in 2-propanol. J. Chem. Phys. 98:6257-6262.
    • (1993) J. Chem. Phys. , vol.98 , pp. 6257-6262
    • Terazima, M.1    Hirota, N.2
  • 27
    • 0000684896 scopus 로고
    • Translational diffusion of transient radicals created by the photoinduced hydrogen abstraction reaction in solution - Anomalous size dependence in the radical diffusion
    • Terazima, M., K. Okamoto, and N. Hirota. 1995. Translational diffusion of transient radicals created by the photoinduced hydrogen abstraction reaction in solution - anomalous size dependence in the radical diffusion. J. Chem. Phys. 102:2506-2515.
    • (1995) J. Chem. Phys. , vol.102 , pp. 2506-2515
    • Terazima, M.1    Okamoto, K.2    Hirota, N.3
  • 28
    • 0033785811 scopus 로고    scopus 로고
    • Is the translational diffusion of organic radicals different from that of closed-shell molecules?
    • Terazima, M. 2000. Is the translational diffusion of organic radicals different from that of closed-shell molecules? Acc. Chem. Res. 33:687-694.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 687-694
    • Terazima, M.1
  • 29
    • 0042823423 scopus 로고    scopus 로고
    • A novel methods for study of protein folding kinetics by monitoring diffusion coefficient in time domain
    • Nada, T., and M. Terazima. 2003. A novel methods for study of protein folding kinetics by monitoring diffusion coefficient in time domain. Biophys. J. 85:1876-1881.
    • (2003) Biophys. J. , vol.85 , pp. 1876-1881
    • Nada, T.1    Terazima, M.2
  • 30
    • 0029328350 scopus 로고
    • A simple and improved method of isolation and purification for native oat phytochrome
    • Lapko, V. N., and P.-S. Song. 1995. A simple and improved method of isolation and purification for native oat phytochrome. Photochem. Photobiol. 62:194-198.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 194-198
    • Lapko, V.N.1    Song, P.-S.2
  • 31
    • 0022431885 scopus 로고
    • Structure function studies on phytochrome
    • Lagarias, J. C., and F. M. Mercurio. 1985. Structure function studies on phytochrome. J. Biol. Chem. 260:2415-2423.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2415-2423
    • Lagarias, J.C.1    Mercurio, F.M.2
  • 32
    • 0035497692 scopus 로고    scopus 로고
    • Time-resolved thermodynamic analysis of the oat phytochrome A phototransformation. A photothermal beam deflection study
    • Michler, I., and S. E. Braslavsky. 2001. Time-resolved thermodynamic analysis of the oat phytochrome A phototransformation. A photothermal beam deflection study. Photochem. Photobiol. 74:624-635.
    • (2001) Photochem. Photobiol. , vol.74 , pp. 624-635
    • Michler, I.1    Braslavsky, S.E.2
  • 33
    • 0037357714 scopus 로고    scopus 로고
    • A novel correlation for protein diffusion coefficients based on molecular weight and radius of gyration
    • Hem, L. H., and B. Niemeyer. 2003. A novel correlation for protein diffusion coefficients based on molecular weight and radius of gyration. Biotechnol. Prog. 19:544-548.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 544-548
    • Hem, L.H.1    Niemeyer, B.2
  • 34
    • 33745728296 scopus 로고    scopus 로고
    • Tetramer formation kinetics in the signaling state of AppA monitored by the time-resolved diffusion
    • Hazra, P., K. Inoue, W. Laan, J. Hellingwerf, and M. Terazima. 2006. Tetramer formation kinetics in the signaling state of AppA monitored by the time-resolved diffusion. Biophys. J. 91:654-661.
    • (2006) Biophys. J. , vol.91 , pp. 654-661
    • Hazra, P.1    Inoue, K.2    Laan, W.3    Hellingwerf, J.4    Terazima, M.5
  • 35
    • 33745686031 scopus 로고    scopus 로고
    • Kinetic measurement of transient dimerization and dissociation reactions of Arabidopsis phototropin 1 LOV2 domain
    • Nakasone, Y., T. Eitoku, D. Matsuoka, S. Tokutomi, and M. Terazima. 2006. Kinetic measurement of transient dimerization and dissociation reactions of Arabidopsis phototropin 1 LOV2 domain. Biophys. J. 91:645-653.
    • (2006) Biophys. J. , vol.91 , pp. 645-653
    • Nakasone, Y.1    Eitoku, T.2    Matsuoka, D.3    Tokutomi, S.4    Terazima, M.5
  • 36
    • 29144472913 scopus 로고    scopus 로고
    • Diffusion coefficient and the secondary structure of poly-L-glutamic acid in aqueous solution
    • Inoue, K., N. Baden, and M. Terazima. 2005. Diffusion coefficient and the secondary structure of poly-L-glutamic acid in aqueous solution. J. Phys. Chem. B. 109:22623-22628.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 22623-22628
    • Inoue, K.1    Baden, N.2    Terazima, M.3
  • 37
    • 0001120129 scopus 로고    scopus 로고
    • Correlation dimension as a measure of surface roughness of protein molecules
    • Choi, J. H., H. Kim, and S. Lee. 1998. Correlation dimension as a measure of surface roughness of protein molecules. J. Chem. Phys. 109:7001-7004.
    • (1998) J. Chem. Phys. , vol.109 , pp. 7001-7004
    • Choi, J.H.1    Kim, H.2    Lee, S.3
  • 38
    • 0032724828 scopus 로고    scopus 로고
    • Light quality-dependent nuclear import of the plant photoreceptors phytochrome A and B
    • Kircher, S., L. Kozma-Bognar, L. Kim, E. Adam, K. Harter, E. Schafer, and F. Nagy. 1999. Light quality-dependent nuclear import of the plant photoreceptors phytochrome A and B. Plant Cell. 11:1445-1456.
    • (1999) Plant Cell. , vol.11 , pp. 1445-1456
    • Kircher, S.1    Kozma-Bognar, L.2    Kim, L.3    Adam, E.4    Harter, K.5    Schafer, E.6    Nagy, F.7
  • 39
    • 0030295130 scopus 로고    scopus 로고
    • Nuclear localization activity of phytochrome B
    • Sakamoto, K., and A. Nagatani. 1996. Nuclear localization activity of phytochrome B. Plant J. 10:859-868.
    • (1996) Plant J. , vol.10 , pp. 859-868
    • Sakamoto, K.1    Nagatani, A.2
  • 40
    • 0029040034 scopus 로고
    • Phytochromes - Photosensory perception and signal-transduction
    • Quail, P. H., M. T. Boylan, B. M. Parks, T. W. Short, Y. Xu, and D. Wagner. 1995. Phytochromes - photosensory perception and signal-transduction. Science. 268:675-680.
    • (1995) Science , vol.268 , pp. 675-680
    • Quail, P.H.1    Boylan, M.T.2    Parks, B.M.3    Short, T.W.4    Xu, Y.5    Wagner, D.6
  • 41
    • 0000632275 scopus 로고    scopus 로고
    • Measurement of mass diffusion coefficients using nonexponential forced Rayleigh scattering signals
    • Spiegel, D. R., A. H. Marshall, N. T. Jukam, H. S. Park, and T. Chang. 1998. Measurement of mass diffusion coefficients using nonexponential forced Rayleigh scattering signals. J. Chem. Phys. 109:267-274.
    • (1998) J. Chem. Phys. , vol.109 , pp. 267-274
    • Spiegel, D.R.1    Marshall, A.H.2    Jukam, N.T.3    Park, H.S.4    Chang, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.