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Volumn 3, Issue 11, 2014, Pages 811-819

Biophysical, mutational, and functional investigation of the chromophore-binding pocket of light-oxygen-voltage photoreceptors

Author keywords

Absorption spectroscopy; Electron paramagnetic resonance; Light oxygen voltage; Optogenetics; Photocycle; Photoreceptor; Signal transduction

Indexed keywords

LIGHT OXYGEN VOLTAGE PHOTORECEPTOR PROTEIN; PEPTIDES AND PROTEINS; PHOTOTROPIN; PROTEIN YP1; UNCLASSIFIED DRUG;

EID: 84912108174     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/sb400205x     Document Type: Article
Times cited : (28)

References (42)
  • 1
    • 44949122636 scopus 로고    scopus 로고
    • Algal sensory photoreceptors
    • Hegemann, P. (2008) Algal sensory photoreceptors. Annu. Rev. Plant Biol. 59, 167-189.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 167-189
    • Hegemann, P.1
  • 2
    • 78650885619 scopus 로고    scopus 로고
    • Engineered photoreceptors as novel optogenetic tools
    • Möglich, A., and Moffat, K. (2010) Engineered photoreceptors as novel optogenetic tools. Photochem. Photobiol. Sci. 9, 1286-1300.
    • (2010) Photochem. Photobiol. Sci. , vol.9 , pp. 1286-1300
    • Möglich, A.1    Moffat, K.2
  • 3
    • 33749848951 scopus 로고    scopus 로고
    • Next-generation optical technologies for illuminating genetically targeted brain circuits
    • Deisseroth, K., Feng, G., Majewska, A. K., Miesenböck, G., Ting, A., and Schnitzer, M. J. (2006) Next-generation optical technologies for illuminating genetically targeted brain circuits. J. Neurosci. 26, 10380-10386.
    • (2006) J. Neurosci. , vol.26 , pp. 10380-10386
    • Deisseroth, K.1    Feng, G.2    Majewska, A.K.3    Miesenböck, G.4    Ting, A.5    Schnitzer, M.J.6
  • 6
    • 69949104482 scopus 로고    scopus 로고
    • A genetically encoded photoactivatable Rac controls the motility of living cells
    • Wu, Y. I., Frey, D., Lungu, O. I., Jaehrig, A., Schlichting, I., Kuhlman, B., and Hahn, K. M. (2009) A genetically encoded photoactivatable Rac controls the motility of living cells. Nature 461, 104-108.
    • (2009) Nature , vol.461 , pp. 104-108
    • Wu, Y.I.1    Frey, D.2    Lungu, O.I.3    Jaehrig, A.4    Schlichting, I.5    Kuhlman, B.6    Hahn, K.M.7
  • 7
    • 58549105950 scopus 로고    scopus 로고
    • Design and signaling mechanism of light-regulated histidine kinases
    • Möglich, A., Ayers, R. A., and Moffat, K. (2009) Design and signaling mechanism of light-regulated histidine kinases. J. Mol. Biol. 385, 1433-1444.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1433-1444
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 9
    • 80052968825 scopus 로고    scopus 로고
    • Function, structure and mechanism of bacterial photosensory LOV proteins
    • Herrou, J., and Crosson, S. (2011) Function, structure and mechanism of bacterial photosensory LOV proteins. Nat. Rev. Microbiol. 9, 713-723.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 713-723
    • Herrou, J.1    Crosson, S.2
  • 10
    • 0037306223 scopus 로고    scopus 로고
    • Phot-LOV1: Photocycle of a blue-light receptor domain from the green alga Chlamydomonas reinhardtii
    • Kottke, T., Heberle, J., Hehn, D., Dick, B., and Hegemann, P. (2003) Phot-LOV1: Photocycle of a blue-light receptor domain from the green alga Chlamydomonas reinhardtii. Biophys. J. 84, 1192-1201.
    • (2003) Biophys. J. , vol.84 , pp. 1192-1201
    • Kottke, T.1    Heberle, J.2    Hehn, D.3    Dick, B.4    Hegemann, P.5
  • 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
    • 47649085005 scopus 로고    scopus 로고
    • Estimation of the available free energy in a LOV2-J α photoswitch
    • Yao, X., Rosen, M. K., and Gardner, K. H. (2008) Estimation of the available free energy in a LOV2-J α photoswitch. Nat. Chem. Biol. 4, 491-497.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 491-497
    • Yao, X.1    Rosen, M.K.2    Gardner, K.H.3
  • 16
    • 0035937443 scopus 로고    scopus 로고
    • Two-state allosteric behavior in a single-domain signaling protein
    • Volkman, B. F., Lipson, D., Wemmer, D. E., and Kern, D. (2001) Two-state allosteric behavior in a single-domain signaling protein. Science 291, 2429-2433.
    • (2001) Science , vol.291 , pp. 2429-2433
    • Volkman, B.F.1    Lipson, D.2    Wemmer, D.E.3    Kern, D.4
  • 17
    • 54249116230 scopus 로고
    • Genetic regulatory mechanisms in the synthesis of proteins
    • Jacob, F., and Monod, J. (1961) Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3, 318-356.
    • (1961) J. Mol. Biol. , vol.3 , pp. 318-356
    • Jacob, F.1    Monod, J.2
  • 18
    • 70349777587 scopus 로고    scopus 로고
    • Structure and signaling mechanism of Per-ARNT-Sim domains
    • Möglich, A., Ayers, R. A., and Moffat, K. (2009) Structure and signaling mechanism of Per-ARNT-Sim domains. Structure 17, 1282-1294.
    • (2009) Structure , vol.17 , pp. 1282-1294
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 20
    • 70350340730 scopus 로고    scopus 로고
    • Mechanism-based tuning of a LOV domain photoreceptor
    • Zoltowski, B. D., Vaccaro, B., and Crane, B. R. (2009) Mechanism-based tuning of a LOV domain photoreceptor. Nat. Chem. Biol. 5, 827-834.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 827-834
    • Zoltowski, B.D.1    Vaccaro, B.2    Crane, B.R.3
  • 21
    • 79953678110 scopus 로고    scopus 로고
    • Modulation of the photocycle of a LOV domain photoreceptor by the hydrogen-bonding network
    • Raffelberg, S., Mansurova, M., Gärtner, W., and Losi, A. (2011) Modulation of the photocycle of a LOV domain photoreceptor by the hydrogen-bonding network. J. Am. Chem. Soc. 133, 5346-5356.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5346-5356
    • Raffelberg, S.1    Mansurova, M.2    Gärtner, W.3    Losi, A.4
  • 22
    • 84885571783 scopus 로고    scopus 로고
    • Charting the signal trajectory in a light-oxygen-voltage photoreceptor by
    • random mutagenesis and covariance analysis.
    • Gleichmann, T., Diensthuber, R. P., and Möglich, A. (2013) Charting the signal trajectory in a light-oxygen-voltage photoreceptor by random mutagenesis and covariance analysis. J. Biol. Chem. 288, 29345-29355.
    • (2013) J. Biol. Chem. , vol.288 , pp. 29345-29355
    • Gleichmann, T.1    Diensthuber, R.P.2    Möglich, A.3
  • 23
    • 0036224807 scopus 로고    scopus 로고
    • First evidence for phototropin-related blue-light receptors in prokaryotes
    • Losi, A., Polverini, E., Quest, B., and Gärtner, W. (2002) First evidence for phototropin-related blue-light receptors in prokaryotes. Biophys. J. 82, 2627-2634.
    • (2002) Biophys. J. , vol.82 , pp. 2627-2634
    • Losi, A.1    Polverini, E.2    Quest, B.3    Gärtner, W.4
  • 24
    • 84857371657 scopus 로고    scopus 로고
    • From dusk till dawn: One-plasmid systems for light-regulated gene expression
    • Ohlendorf, R., Vidavski, R. R., Eldar, A., Moffat, K., and Möglich, A. (2012) From dusk till dawn: One-plasmid systems for light-regulated gene expression. J. Mol. Biol. 416, 534-542.
    • (2012) J. Mol. Biol. , vol.416 , pp. 534-542
    • Ohlendorf, R.1    Vidavski, R.R.2    Eldar, A.3    Moffat, K.4    Möglich, A.5
  • 25
    • 49449118042 scopus 로고    scopus 로고
    • Light-activated DNA binding in a designed allosteric protein
    • Strickland, D., Moffat, K., and Sosnick, T. R. (2008) Light-activated DNA binding in a designed allosteric protein. Proc. Natl. Acad. Sci. U.S.A. 105, 10709-10714.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10709-10714
    • Strickland, D.1    Moffat, K.2    Sosnick, T.R.3
  • 27
    • 34250183058 scopus 로고    scopus 로고
    • Phototropin blue-light receptors
    • Christie, J. M. (2007) Phototropin blue-light receptors. Annu. Rev. Plant Biol. 58, 21-45.
    • (2007) Annu. Rev. Plant Biol. , vol.58 , pp. 21-45
    • Christie, J.M.1
  • 28
    • 72049103147 scopus 로고    scopus 로고
    • Domain swapping to assess the mechanistic basis of Arabidopsis phototropin 1 receptor kinase activation and endocytosis by blue light
    • Kaiserli, E., Sullivan, S., Jones, M. A., Feeney, K. A., and Christie, J. M. (2009) Domain swapping to assess the mechanistic basis of Arabidopsis phototropin 1 receptor kinase activation and endocytosis by blue light. Plant Cell 21, 3226-3244.
    • (2009) Plant Cell , vol.21 , pp. 3226-3244
    • Kaiserli, E.1    Sullivan, S.2    Jones, M.A.3    Feeney, K.A.4    Christie, J.M.5
  • 31
    • 37049002915 scopus 로고    scopus 로고
    • N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa
    • Halavaty, A. S., and Moffat, K. (2007) N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue light sensor phototropin 1 from Avena sativa. Biochemistry 46, 14001-14009.
    • (2007) Biochemistry , vol.46 , pp. 14001-14009
    • Halavaty, A.S.1    Moffat, K.2
  • 32
    • 84879836986 scopus 로고    scopus 로고
    • Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators
    • Diensthuber, R. P., Bommer, M., Gleichmann, T., and Möglich, A. (2013) Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators. Structure 21, 1127-1136.
    • (2013) Structure , vol.21 , pp. 1127-1136
    • Diensthuber, R.P.1    Bommer, M.2    Gleichmann, T.3    Möglich, A.4
  • 33
    • 84860285055 scopus 로고    scopus 로고
    • The amino-terminal helix modulates light-activated conformational changes in AsLOV2
    • Zayner, J. P., Antoniou, C., and Sosnick, T. R. (2012) The amino-terminal helix modulates light-activated conformational changes in AsLOV2. J. Mol. Biol. 419, 61-74.
    • (2012) J. Mol. Biol. , vol.419 , pp. 61-74
    • Zayner, J.P.1    Antoniou, C.2    Sosnick, T.R.3
  • 34
    • 33947377466 scopus 로고    scopus 로고
    • A base-catalyzed mechanism for dark state recovery in the Avena sativa phototropin-1 LOV2 domain
    • Alexandre, M. T., Arents, J. C., van Grondelle, R., Hellingwerf, K. J., and Kennis, J. T. (2007) A base-catalyzed mechanism for dark state recovery in the Avena sativa phototropin-1 LOV2 domain. Biochemistry 46, 3129-3137.
    • (2007) Biochemistry , vol.46 , pp. 3129-3137
    • Alexandre, M.T.1    Arents, J.C.2    Van Grondelle, R.3    Hellingwerf, K.J.4    Kennis, J.T.5
  • 35
    • 84899910793 scopus 로고    scopus 로고
    • Factors that control the chemistry of the LOV domain photocycle
    • Zayner, J. P., and Sosnick, T. R. (2014) Factors that control the chemistry of the LOV domain photocycle. PLoS One 9, e87074.
    • (2014) PLoS One , vol.9 , pp. e87074
    • Zayner, J.P.1    Sosnick, T.R.2
  • 36
    • 84888086103 scopus 로고    scopus 로고
    • The amino acids surrounding the flavin 7a-methyl group determine the UVA spectral features of a LOV protein
    • Raffelberg, S., Gutt, A., Gärtner, W., Mandalari, C., Abbruzzetti, S., Viappiani, C., and Losi, A. (2013) The amino acids surrounding the flavin 7a-methyl group determine the UVA spectral features of a LOV protein. Biol. Chem. 394, 1517-1528.
    • (2013) Biol. Chem. , vol.394 , pp. 1517-1528
    • Raffelberg, S.1    Gutt, A.2    Gärtner, W.3    Mandalari, C.4    Abbruzzetti, S.5    Viappiani, C.6    Losi, A.7
  • 37
    • 84882982790 scopus 로고    scopus 로고
    • Investigating models of protein function and allostery with a widespread mutational analysis of a light-activated protein
    • Zayner, J. P., Antoniou, C., French, A. R., Hause, R. J., Jr., and Sosnick, T. R. (2013) Investigating models of protein function and allostery with a widespread mutational analysis of a light-activated protein. Biophys. J. 105, 1027-1036.
    • (2013) Biophys. J. , vol.105 , pp. 1027-1036
    • Zayner, J.P.1    Antoniou, C.2    French, A.R.3    Hause, R.J.4    Sosnick, T.R.5
  • 38
    • 80054763468 scopus 로고    scopus 로고
    • Variations in protein-flavin hydrogen bonding in a light, oxygen, voltage domain produce non-Arrhenius kinetics of adduct decay
    • Zoltowski, B. D., Nash, A. I., and Gardner, K. H. (2011) Variations in protein-flavin hydrogen bonding in a light, oxygen, voltage domain produce non-Arrhenius kinetics of adduct decay. Biochemistry 50, 8771-8779.
    • (2011) Biochemistry , vol.50 , pp. 8771-8779
    • Zoltowski, B.D.1    Nash, A.I.2    Gardner, K.H.3
  • 40
    • 58549088979 scopus 로고    scopus 로고
    • In vivo generation of flavoproteins with modified cofactors
    • Mathes, T., Vogl, C., Stolz, J., and Hegemann, P. (2009) In vivo generation of flavoproteins with modified cofactors. J. Mol. Biol. 385, 1511-1518.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1511-1518
    • Mathes, T.1    Vogl, C.2    Stolz, J.3    Hegemann, P.4
  • 41
    • 84893187199 scopus 로고    scopus 로고
    • Fluorescence Imaging-based high-throughput screening of fast- and slow-cycling LOV proteins
    • Kawano, F., Aono, Y., Suzuki, H., and Sato, M. (2013) Fluorescence Imaging-based high-throughput screening of fast- and slow-cycling LOV proteins. PLoS One 8, e82693.
    • (2013) PLoS One , vol.8 , pp. e82693
    • Kawano, F.1    Aono, Y.2    Suzuki, H.3    Sato, M.4
  • 42
    • 74049123767 scopus 로고    scopus 로고
    • Interdomain signalling in the blue-light sensing and GTP-binding protein YtvA: A mutagenesis study uncovering the importance of specific protein sites
    • Tang, Y., Cao, Z., Livoti, E., Krauss, U., Jaeger, K.-E., Gärtner, W., and Losi, A. (2010) Interdomain signalling in the blue-light sensing and GTP-binding protein YtvA: A mutagenesis study uncovering the importance of specific protein sites. Photochem. Photobiol. Sci. 9, 47-56.
    • (2010) Photochem. Photobiol. Sci. , vol.9 , pp. 47-56
    • Tang, Y.1    Cao, Z.2    Livoti, E.3    Krauss, U.4    Jaeger, K.-E.5    Gärtner, W.6    Losi, A.7


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