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Volumn 43, Issue 51, 2004, Pages 16184-16192

Disruption of the LOV-Jα helix interaction activates phototropin kinase activity

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOCHEMISTRY; CHEMICAL BONDS; OXYGEN; PROTEINS;

EID: 11144344967     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048092i     Document Type: Article
Times cited : (259)

References (32)
  • 1
    • 0033280757 scopus 로고    scopus 로고
    • Blue-light photoreceptors in higher plants
    • Briggs, W. R., and Huala, E. (1999) Blue-light photoreceptors in higher plants, Annu. Rev. Cell Dev. Biol. 15, 33-62.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 33-62
    • Briggs, W.R.1    Huala, E.2
  • 3
    • 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
  • 4
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light photoreceptor, phototropin
    • Salomon, M., Christie, J. M., Knieb, E., Lempert, U., and Briggs, W. R. (2000) Photochemical and mutational analysis of the FMN-binding domains of the plant blue light photoreceptor, 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
  • 6
    • 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
  • 7
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: Insights into light-mediated signal transduction
    • Crosson, S., and Moffat, K. (2001) Structure of a flavin-binding plant photoreceptor domain: insights into light-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
  • 8
    • 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
  • 9
    • 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
  • 10
    • 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
  • 11
    • 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, 8183-91.
    • (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
  • 12
    • 0037428497 scopus 로고    scopus 로고
    • Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of Phototropin 1
    • Corchnoy, S. B., Swartz, T. E., Lewis, J. W., Szundi, I., Briggs, W. R., and Bogomolni, R. A. (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.A.6
  • 13
    • 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
  • 14
    • 1642379708 scopus 로고    scopus 로고
    • Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy
    • Harper, S. M., Neil, L. C., Day, I. J., Hore, P. J., and Gardner, K. H. (2004) Conformational changes in a photosensory LOV domain monitored by time-resolved NMR spectroscopy, J. Am. Chem. Soc. 126, 3390-3391.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3390-3391
    • Harper, S.M.1    Neil, L.C.2    Day, I.J.3    Hore, P.J.4    Gardner, K.H.5
  • 15
    • 84957665033 scopus 로고    scopus 로고
    • (Ishikawa, Y., Oldehoeft, R. R., Reynders, J. V. W., and Tholburn, M., Eds.), Springer, Berlin
    • Bashford, D. (1997) in Scientific computing in object-oriented parallel environments (Ishikawa, Y., Oldehoeft, R. R., Reynders, J. V. W., and Tholburn, M., Eds.) pp 233-240, Springer, Berlin.
    • (1997) Scientific Computing in Object-Oriented Parallel Environments , pp. 233-240
    • Bashford, D.1
  • 16
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., Hess, B., and van der Spoel, D. (2001) GROMACS 3.0: A package for molecular simulation and trajectory analysis, J. Mol. Mod. 7, 306-317.
    • (2001) J. Mol. Mod. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 19
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T., and Wells, J. A. (1995) A hot spot of binding energy in a hormone-receptor interface, Science 267, 383-6.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 20
    • 0037062577 scopus 로고    scopus 로고
    • Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domain of the plant blue-light receptor phototropin 1
    • Swartz, T. E., Wenzel, P. J., Corchnoy, S. B., Briggs, W. R., and Bogomolni, R. A. (2002) Vibration spectroscopy reveals light-induced chromophore and protein structural changes in the LOV2 domain 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.A.5
  • 21
    • 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., and 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
  • 22
    • 4143081643 scopus 로고    scopus 로고
    • Dimerization of the plant photoreceptor phototropin is probably mediated by the LOV1 domain
    • Salomon, M., Lempert, U., and Rudiger, W. (2004) Dimerization 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    Rudiger, W.3
  • 23
    • 3142617400 scopus 로고    scopus 로고
    • Role of Gln1029 in the photoactivation processes of the LOV2 domain in Adiantum phytochrome3
    • Nozaki, D., Iwata, T., Ishikawa, T., Todo, T., Tokutomi, S., and Kandori, H. (2004) Role of Gln1029 in the photoactivation processes of the LOV2 domain in Adiantum phytochrome3, Biochemistry 43, 8373-8379.
    • (2004) Biochemistry , vol.43 , pp. 8373-8379
    • Nozaki, D.1    Iwata, T.2    Ishikawa, T.3    Todo, T.4    Tokutomi, S.5    Kandori, H.6
  • 24
    • 0033524943 scopus 로고    scopus 로고
    • Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
    • Huse, M., Chen, Y. G., Massague, J., and Kuriyan, J. (1999) Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12, Cell 96, 425-36.
    • (1999) Cell , vol.96 , pp. 425-436
    • Huse, M.1    Chen, Y.G.2    Massague, J.3    Kuriyan, J.4
  • 25
    • 0037446727 scopus 로고    scopus 로고
    • Mapping of low- and high-fluence autophosphorylation sites in phototropin 1
    • Salomon, M., Knieb, E., Zeppelin, T., and Rudiger, W. (2003) Mapping of low- and high-fluence autophosphorylation sites in phototropin 1, Biochemistry 42, 4217-4225.
    • (2003) Biochemistry , vol.42 , pp. 4217-4225
    • Salomon, M.1    Knieb, E.2    Zeppelin, T.3    Rudiger, W.4
  • 26
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by Hydrophobic motif phosphorylation
    • Yang, J., Cron, P., Thompson, V., Good, V. M., Hess, D., Hemmings, B. A., and Barford, D. (2002) Molecular mechanism for the regulation of protein kinase B/Akt by Hydrophobic motif phosphorylation, Mol. Cell 9, 1227-40.
    • (2002) Mol. Cell , vol.9 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 27
    • 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
  • 28
    • 0029918062 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
    • Bourne, Y., Watson, M. H., Mickey, M. J., Holmes, W., Rocque, W., Reed, S. I., and Tainer, J. A. (1996) Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1, Cell 84, 863-74.
    • (1996) Cell , vol.84 , pp. 863-874
    • Bourne, Y.1    Watson, M.H.2    Mickey, M.J.3    Holmes, W.4    Rocque, W.5    Reed, S.I.6    Tainer, J.A.7
  • 29
    • 0346734132 scopus 로고    scopus 로고
    • Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor
    • Erbel, P. J., Card, P. B., Karakuzu, O., Bruick, R. K., and Gardner, K. H. (2003) Structural basis for PAS domain heterodimerization in the basic helix-loop-helix-PAS transcription factor hypoxia-inducible factor, Proc. Natl. Acad. Sci. U.S.A. 100, 15504-9.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 15504-15509
    • Erbel, P.J.1    Card, P.B.2    Karakuzu, O.3    Bruick, R.K.4    Gardner, K.H.5
  • 30
    • 2442624510 scopus 로고    scopus 로고
    • A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor
    • Kurokawa, H., Lee, D. S., Watanabe, M., Sagami, I., Mikami, B., Raman, C. S., and Shimizu, T. (2004) A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor, J. Biol. Chem. 279, 20186-93.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20186-20193
    • Kurokawa, H.1    Lee, D.S.2    Watanabe, M.3    Sagami, I.4    Mikami, B.5    Raman, C.S.6    Shimizu, T.7
  • 32
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet, F. (1988) Multiple sequence alignment with hierarchical clustering, Nucleic Acids Res. 16, 10881-10890.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1


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