메뉴 건너뛰기




Volumn 132, Issue 7, 2013, Pages 1-11

Theoretical prediction of the protein-protein interaction between Arabidopsis thaliana COP1 and UVR8

Author keywords

Arabidopsis thaliana; COP1; Docking; Modeling; Mutation; Protein protein interaction; UVR8; WD40

Indexed keywords


EID: 84877088330     PISSN: 1432881X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00214-013-1371-7     Document Type: Article
Times cited : (9)

References (45)
  • 1
    • 84878793556 scopus 로고    scopus 로고
    • UV-Bexposure,ROSand stress: Inseparable companions or loosely linked associates?
    • in press. doi: 10.1021/ci300264u
    • Hideg É, Jansen MAK, Strid Å.(2012)UV-Bexposure,ROSand stress: inseparable companions or loosely linked associates? Trends Plant Sci, in press. doi: 10.1021/ci300264u
    • (2012) Trends Plant Sci
    • Hideg, É.1    Jansen, M.A.K.2    Strid, Å.3
  • 2
    • 84866444128 scopus 로고    scopus 로고
    • UV-B induced morphogenesis: Four players or a quartet?
    • Jansen MAK, Coffey AM, Prinsen E (2012) UV-B induced morphogenesis: four players or a quartet? Plant Signal Behav 7:1185-1187
    • (2012) Plant Signal Behav , vol.7 , pp. 1185-1187
    • Jansen, M.A.K.1    Coffey, A.M.2    Prinsen, E.3
  • 6
    • 38949188735 scopus 로고    scopus 로고
    • UV-B signaling pathways with different fluence-rate response profiles are distinguished in mature Arabidopsis leaf tissue by requirement for UVR8, HY5, and HYH
    • Brown BA, Jenkins GI (2008) UV-B signaling pathways with different fluence-rate response profiles are distinguished in mature Arabidopsis leaf tissue by requirement for UVR8, HY5, and HYH. Plant Physiol 146:576-588
    • (2008) Plant Physiol , vol.146 , pp. 576-588
    • Brown, B.A.1    Jenkins, G.I.2
  • 7
    • 35348841586 scopus 로고    scopus 로고
    • UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific signaling component UVR8 and activates its function in the nucleus
    • Kaiserli E, Jenkins GI (2007) UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific signaling component UVR8 and activates its function in the nucleus. Plant Cell 19:2662-2673
    • (2007) Plant Cell , vol.19 , pp. 2662-2673
    • Kaiserli, E.1    Jenkins, G.I.2
  • 8
    • 66449126361 scopus 로고    scopus 로고
    • Signal transduction in responses to UV-B radiation
    • Jenkins GI (2009) Signal transduction in responses to UV-B radiation. Annu Rev Plant Biol 60:407-431
    • (2009) Annu Rev Plant Biol , vol.60 , pp. 407-431
    • Jenkins, G.I.1
  • 9
    • 79959769246 scopus 로고    scopus 로고
    • Computational Evidence for the role of Arabidopsis thaliana UVR8 as UV-B photoreceptor and identification of its chromophore amino acids
    • Wu M, Grahn E, Eriksson LA, Strid (2011) Computational Evidence for the role of Arabidopsis thaliana UVR8 as UV-B photoreceptor and identification of its chromophore amino acids. J Chem Inf Model 51:1287-1295
    • (2011) J Chem Inf Model , vol.51 , pp. 1287-1295
    • Wu, M.1    Grahn, E.2    Eriksson, L.A.3
  • 13
    • 27744474619 scopus 로고    scopus 로고
    • COP1-from plant photomorphogenesis to mammalian tumorigenesis
    • Yi C, Deng XW (2005) COP1-from plant photomorphogenesis to mammalian tumorigenesis. Trends Cell Biol 15:618-625
    • (2005) Trends Cell Biol , vol.15 , pp. 618-625
    • Yi, C.1    Deng, X.W.2
  • 15
    • 0028429180 scopus 로고
    • Regulatory hierarchy of photomorphogenic loci: Allele-specific and light-dependent interaction between the HY5 and COP1 loci
    • Ang LH, Deng XW (1994) Regulatory hierarchy of photomorphogenic loci: allele-specific and light-dependent interaction between the HY5 and COP1 loci. Plant Cell 6:613-628
    • (1994) Plant Cell , vol.6 , pp. 613-628
    • Ang, L.H.1    Deng, X.W.2
  • 16
    • 0028410547 scopus 로고
    • Genetic and molecular analysis of an allelic series of cop1 mutants suggests functional roles for the multiple protein domains
    • McNellis TW, von Arnim AG, Araki T, Komeda Y, Miséra S, Deng XW (1994) Genetic and molecular analysis of an allelic series of cop1 mutants suggests functional roles for the multiple protein domains. Plant Cell 6:487-500
    • (1994) Plant Cell , vol.6 , pp. 487-500
    • McNellis, T.W.1    von Arnim, A.G.2    Araki, T.3    Komeda, Y.4    Miséra, S.5    Deng, X.W.6
  • 17
    • 0028519924 scopus 로고
    • Overexpression of Arabidopsis COP1 results in partial suppression of lightmediated development: Evidence for a light-inactivable repressor of photomorphogenesis
    • McNellis TW, von Arnim AG, Deng XW (1994) Overexpression of Arabidopsis COP1 results in partial suppression of lightmediated development: evidence for a light-inactivable repressor of photomorphogenesis. Plant Cell 6:1391-1400
    • (1994) Plant Cell , vol.6 , pp. 1391-1400
    • McNellis, T.W.1    von Arnim, A.G.2    Deng, X.W.3
  • 18
    • 0026454289 scopus 로고
    • COP1, an Arabidopsis regulatory gene, encodes a protein with both a zinc-binding motif and a G beta homologous domain
    • Deng XW, Matsui M, Wei N, Wagner D, Chu AM, Feldmann KA, Quail PH (1992) COP1, an Arabidopsis regulatory gene, encodes a protein with both a zinc-binding motif and a G beta homologous domain. Cell 71:791-801
    • (1992) Cell , vol.71 , pp. 791-801
    • Deng, X.W.1    Matsui, M.2    Wei, N.3    Wagner, D.4    Chu, A.M.5    Feldmann, K.A.6    Quail, P.H.7
  • 19
    • 4544232080 scopus 로고    scopus 로고
    • The SPA quartet: A family of WD-repeat proteins with a central role in suppression of photomorphogenesis in arabidopsis
    • Laubinger S, Fittinghoff K, Hoecker U (2004) The SPA quartet: a family of WD-repeat proteins with a central role in suppression of photomorphogenesis in arabidopsis. Plant Cell 16:2293-2306
    • (2004) Plant Cell , vol.16 , pp. 2293-2306
    • Laubinger, S.1    Fittinghoff, K.2    Hoecker, U.3
  • 20
    • 0037093378 scopus 로고    scopus 로고
    • Two interacting bZIP proteins are direct targets of COP1-mediated control of lightdependent gene expression in Arabidopsis
    • Holm M, Ma LG, Qu LJ, Deng XW (2002) Two interacting bZIP proteins are direct targets of COP1-mediated control of lightdependent gene expression in Arabidopsis. Genes Dev 16:1247-1259
    • (2002) Genes Dev , vol.16 , pp. 1247-1259
    • Holm, M.1    Ma, L.G.2    Qu, L.J.3    Deng, X.W.4
  • 21
    • 0035543363 scopus 로고    scopus 로고
    • The signaling mechanism of Arabidopsis CRY1 involves direct interaction with COP1
    • Yang HQ, Tang RH, Cashmore AR (2001) The signaling mechanism of Arabidopsis CRY1 involves direct interaction with COP1. Plant Cell 13:2573-2587
    • (2001) Plant Cell , vol.13 , pp. 2573-2587
    • Yang, H.Q.1    Tang, R.H.2    Cashmore, A.R.3
  • 22
    • 0035863052 scopus 로고    scopus 로고
    • Identification of a structural motif that confers specific interaction with the WD40 repeat domain of Arabidopsis COP1
    • Holm M, Hardtke CS, Gaudet R, Deng XW (2001) Identification of a structural motif that confers specific interaction with the WD40 repeat domain of Arabidopsis COP1. EMBO J 20:118-127
    • (2001) EMBO J , vol.20 , pp. 118-127
    • Holm, M.1    Hardtke, C.S.2    Gaudet, R.3    Deng, X.W.4
  • 23
    • 0034993094 scopus 로고    scopus 로고
    • Protein folds propelled by diversity
    • Paoli M (2001) Protein folds propelled by diversity. Prog Biophys Mol Biol 76:103-130
    • (2001) Prog Biophys Mol Biol , vol.76 , pp. 103-130
    • Paoli, M.1
  • 25
    • 0028170530 scopus 로고
    • Groucho is required for Drosophila neurogenesis, segmentation, and sex determination and interacts directly with hairy-related bHLH proteins
    • Paroush Z, Finley RL Jr, Kidd T, Wainwright SM, Ingham PW, Brent R, Ish-Horowicz D (1994) Groucho is required for Drosophila neurogenesis, segmentation, and sex determination and interacts directly with hairy-related bHLH proteins. Cell 79:805-815
    • (1994) Cell , vol.79 , pp. 805-815
    • Paroush, Z.1    Finley Jr., R.L.2    Kidd, T.3    Wainwright, S.M.4    Ingham, P.W.5    Brent, R.6    Ish-Horowicz, D.7
  • 27
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA: A selfparameterizing force field
    • Krieger E, Koraimann G, Vriend G (2002) Increasing the precision of comparative models with YASARA NOVA: a selfparameterizing force field. Proteins 47:393-402
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 28
    • 58049201719 scopus 로고    scopus 로고
    • WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket
    • Song JJ, Kingston RE (2008) WDR5 interacts with mixed lineage leukemia (MLL) protein via the histone H3-binding pocket. J Biol Chem 283:35258-35264
    • (2008) J Biol Chem , vol.283 , pp. 35258-35264
    • Song, J.J.1    Kingston, R.E.2
  • 30
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4:435-447
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 31
    • 0242663237 scopus 로고    scopus 로고
    • A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations
    • Duan Y, Wu C, Chowdhury S, Lee MC, Xiong G, Zhang W, Yang R, Cieplak P, Luo R, Lee T et al (2003) A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations. J Comput Chem 24:1999-2012
    • (2003) J Comput Chem , vol.24 , pp. 1999-2012
    • Duan, Y.1    Wu, C.2    Chowdhury, S.3    Lee, M.C.4    Xiong, G.5    Zhang, W.6    Yang, R.7    Cieplak, P.8    Luo, R.9    Lee, T.10
  • 32
    • 36449007976 scopus 로고
    • The effect of long electrostatic interactions in simulations of macromolecular crystals: A comparison of the Ewald and truncated list methods
    • York DM, Darden TA, Pedersen LG (1993) The effect of long electrostatic interactions in simulations of macromolecular crystals: a comparison of the Ewald and truncated list methods. J Chem Phys 99:8345-8348
    • (1993) J Chem Phys , vol.99 , pp. 8345-8348
    • York, D.M.1    Darden, T.A.2    Pedersen, L.G.3
  • 34
    • 0019707626 scopus 로고
    • Polymorphic transitions in single-crystals: A new molecular-dynamics method
    • Parrinello M, Rahman A (1981) Polymorphic transitions in single-crystals: a new molecular-dynamics method. J Appl Phys 52:7182-7190
    • (1981) J Appl Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 36
    • 84855757480 scopus 로고    scopus 로고
    • MOE 2011.10, Chemical Computing Group, Montreal, Canada
    • Molecular Operating Environment, MOE 2011.10 (2012) Chemical Computing Group, Montreal, Canada
    • (2012) Molecular Operating Environment
  • 37
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulate annealing and Bayesian scoring functions
    • Simons KT, Kooperberg C, Huang E, Baker D (1997) Assembly of protein tertiary structures from fragments with similar local sequences using simulate annealing and Bayesian scoring functions. J Mol Biol 268:209-225
    • (1997) J Mol Biol , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 38
    • 0032929780 scopus 로고    scopus 로고
    • Improved recognition of native-like protein structures using a combination of sequence-dependent and sequence-independent features of proteins
    • Simons KT, Ruczinski I, Kooperberg C, Fox B, Bystroff C, Baker D (1999) Improved recognition of native-like protein structures using a combination of sequence-dependent and sequence-independent features of proteins. Proteins 34:82-95
    • (1999) Proteins , vol.34 , pp. 82-95
    • Simons, K.T.1    Ruczinski, I.2    Kooperberg, C.3    Fox, B.4    Bystroff, C.5    Baker, D.6
  • 40
    • 84878770691 scopus 로고    scopus 로고
    • Robetta server
    • Robetta server: http://robetta.bakerlab.org/
  • 42
    • 84865271039 scopus 로고    scopus 로고
    • Variability in docking success rates due to dataset preparation
    • Corbeil CR, Williams CI, Labute P (2012) Variability in docking success rates due to dataset preparation. J Comput Aid Mol Des 26:775-786
    • (2012) J Comput Aid Mol Des , vol.26 , pp. 775-786
    • Corbeil, C.R.1    Williams, C.I.2    Labute, P.3
  • 43
    • 48249088045 scopus 로고    scopus 로고
    • Electrostatic and functional analysis of the seven-bladed WD b-propellers
    • Valeyev NV, Downing AK, Sondek J, Deane C (2008) Electrostatic and functional analysis of the seven-bladed WD b-propellers. Evol Bioinform 4:203-216
    • (2008) Evol Bioinform , vol.4 , pp. 203-216
    • Valeyev, N.V.1    Downing, A.K.2    Sondek, J.3    Deane, C.4
  • 45
    • 0034665253 scopus 로고    scopus 로고
    • HY5 stability and activity in Arabidopsis is regulated by phosphorylation in its COP1 binding domain
    • Hardtke CS, Gohda K, Osterlund MT, Oyama T, Okada K, Deng XW (2000) HY5 stability and activity in Arabidopsis is regulated by phosphorylation in its COP1 binding domain. EMBO J 19:4997-5006
    • (2000) EMBO J , vol.19 , pp. 4997-5006
    • Hardtke, C.S.1    Gohda, K.2    Osterlund, M.T.3    Oyama, T.4    Okada, K.5    Deng, X.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.