메뉴 건너뛰기




Volumn 16, Issue 12, 2004, Pages 3448-3459

Solution structure of the B3 DNA binding domain of the Arabidopsis cold-responsive transcription factor RAV1

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACIDS; DNA; ENZYMES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; TITRATION;

EID: 16244416723     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.104.026112     Document Type: Article
Times cited : (112)

References (44)
  • 1
    • 0030140041 scopus 로고    scopus 로고
    • Early genes and auxin action
    • Abel, S., and Theologis, A. (1996). Early genes and auxin action. Plant Physiol. 111, 9-17.
    • (1996) Plant Physiol. , vol.111 , pp. 9-17
    • Abel, S.1    Theologis, A.2
  • 2
    • 0032530719 scopus 로고    scopus 로고
    • A novel mode of DNA recognition by a β-sheet revealed by the solution structure of the GCC-box binding domain in complex with DNA
    • Allen, M.D., Yamasaki, K., Ohme-Takagi, M., Tateno, M., and Suzuki, M. (1998). A novel mode of DNA recognition by a β-sheet revealed by the solution structure of the GCC-box binding domain in complex with DNA. EMBO J. 17, 5484-5496.
    • (1998) EMBO J. , vol.17 , pp. 5484-5496
    • Allen, M.D.1    Yamasaki, K.2    Ohme-Takagi, M.3    Tateno, M.4    Suzuki, M.5
  • 3
    • 0028019827 scopus 로고
    • Multidimensional nuclear magnetic resonance methods for protein studies
    • Bax, A. (1994). Multidimensional nuclear magnetic resonance methods for protein studies. Curr. Opin. Struct. Biol. 4, 738-744.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 738-744
    • Bax, A.1
  • 4
    • 0027373797 scopus 로고
    • Lactose repressor-operator DNA interactions: Kinetic analysis by a surface plasmon resonance biosensor
    • Bondeson, K., Frostell-Karlsson, A., Fagerstam, L., and Magnusson, G. (1993). Lactose repressor-operator DNA interactions: Kinetic analysis by a surface plasmon resonance biosensor. Anal. Biochem. 214, 245-251.
    • (1993) Anal. Biochem. , vol.214 , pp. 245-251
    • Bondeson, K.1    Frostell-Karlsson, A.2    Fagerstam, L.3    Magnusson, G.4
  • 5
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T., et al. (1998). Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 6
    • 0004195760 scopus 로고    scopus 로고
    • San Francisco: University of California
    • Case, D.A., et al. (2002). AMBER 7. (San Francisco: University of California).
    • (2002) AMBER 7
    • Case, D.A.1
  • 7
    • 0033771325 scopus 로고    scopus 로고
    • Transactivation of the Brassica napus napin promoter by ABI3 requires interaction of the conserved B2 and B3 domains of ABI3 with different cis-elements: B2 mediates activation through an ABRE, whereas B3 interacts with an RY/G-box
    • Ezcurra, I., Wycliffe, P., Nehlin, L., Ellerström, M., and Rask, L. (2000). Transactivation of the Brassica napus napin promoter by ABI3 requires interaction of the conserved B2 and B3 domains of ABI3 with different cis-elements: B2 mediates activation through an ABRE, whereas B3 interacts with an RY/G-box. Plant J. 24, 57-66.
    • (2000) Plant J. , vol.24 , pp. 57-66
    • Ezcurra, I.1    Wycliffe, P.2    Nehlin, L.3    Ellerström, M.4    Rask, L.5
  • 8
    • 0036671216 scopus 로고    scopus 로고
    • Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway
    • Fowler, S., and Thomashow, M.F. (2002). Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway. Plant Cell 14, 1675-1690.
    • (2002) Plant Cell , vol.14 , pp. 1675-1690
    • Fowler, S.1    Thomashow, M.F.2
  • 10
    • 0033592931 scopus 로고    scopus 로고
    • A bZIP factor, TRAB1, interacts with VP1 and mediates abscisic acid-induced transcription
    • Hobo, T., Kowyama, Y., and Hattori, T. (1999). A bZIP factor, TRAB1, interacts with VP1 and mediates abscisic acid-induced transcription. Proc. Natl. Acad. Sci. USA 96, 15348-15353.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 15348-15353
    • Hobo, T.1    Kowyama, Y.2    Hattori, T.3
  • 11
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 12
    • 0033556230 scopus 로고    scopus 로고
    • RAV1, a novel DNA-binding protein, binds to bipartite recognition sequence through two distinct DNA-binding domains uniquely found in higher plants
    • Kagaya, Y., Ohmiya, K., and Hattori, T. (1999). RAV1, a novel DNA-binding protein, binds to bipartite recognition sequence through two distinct DNA-binding domains uniquely found in higher plants. Nucleic Acids Res. 27, 470-478.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 470-478
    • Kagaya, Y.1    Ohmiya, K.2    Hattori, T.3
  • 13
    • 1342285086 scopus 로고    scopus 로고
    • Two mutations in the tetracycline repressor change the inducer anhydrotetracycline to a corepressor
    • Kamionka, A., Bogdanska-Urbaniak, J., Scholz, O., and Hillen, W. (2004). Two mutations in the tetracycline repressor change the inducer anhydrotetracycline to a corepressor. Nucleic Acids Res. 32, 842-847.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 842-847
    • Kamionka, A.1    Bogdanska-Urbaniak, J.2    Scholz, O.3    Hillen, W.4
  • 16
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labelling of milligram quantities of proteins
    • Kigawa, T., Yabuki, T., Yoshida, Y., Tsutsui, M., Ito, Y., Shibata, T., and Yokoyama, S. (1999). Cell-free production and stable-isotope labelling of milligram quantities of proteins. FEBS Lett. 442, 15-19.
    • (1999) FEBS Lett. , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 17
    • 0031942054 scopus 로고    scopus 로고
    • The genetic and molecular dissection of abscisic acid biosynthesis and signal transduction in Arabidopsis
    • Koornneef, M., Leon-Kloosterziel, K.M., Schwarts, S.H., and Zeevaart, J.A.D. (1998). The genetic and molecular dissection of abscisic acid biosynthesis and signal transduction in Arabidopsis. Plant Physiol. Biochem. 36, 83-89.
    • (1998) Plant Physiol. Biochem. , vol.36 , pp. 83-89
    • Koornneef, M.1    Leon-Kloosterziel, K.M.2    Schwarts, S.H.3    Zeevaart, J.A.D.4
  • 18
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996). MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 19
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 20
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmann, J.A., MacArthur, W.M., Kaptein, R., and Thornton, J.M. (1996). AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, W.M.3    Kaptein, R.4    Thornton, J.M.5
  • 22
    • 0024835733 scopus 로고
    • Transposable element induced mutations of the vivapaurous-1 gene of maize
    • McCarty, D.R., Carson, C.B., Lazar, M., and Simonds, S.C. (1989). Transposable element induced mutations of the vivapaurous-1 gene of maize. Dev. Genet. 10, 473-481.
    • (1989) Dev. Genet. , vol.10 , pp. 473-481
    • McCarty, D.R.1    Carson, C.B.2    Lazar, M.3    Simonds, S.C.4
  • 23
    • 0026002971 scopus 로고
    • The vivapaurous-1 developmental gene of maize encodes a novel transcriptional activator
    • McCarty, D.R., Hattori, T., Carson, C.B., Vasil, V., Lazar, M., and Vasil, I.K. (1991). The vivapaurous-1 developmental gene of maize encodes a novel transcriptional activator. Cell 66, 895-905.
    • (1991) Cell , vol.66 , pp. 895-905
    • McCarty, D.R.1    Hattori, T.2    Carson, C.B.3    Vasil, V.4    Lazar, M.5    Vasil, I.K.6
  • 24
    • 0036792684 scopus 로고    scopus 로고
    • EcoRII: A restriction enzyme evolving recombination functions?
    • Mücke, M., Grelle, G., Behlke, J., Kraft, R., Krünger, D.H., and Reuter, M. (2002). EcoRII: A restriction enzyme evolving recombination functions? EMBO J. 21, 5262-5268.
    • (2002) EMBO J. , vol.21 , pp. 5262-5268
    • Mücke, M.1    Grelle, G.2    Behlke, J.3    Kraft, R.4    Krünger, D.H.5    Reuter, M.6
  • 25
    • 0034927781 scopus 로고    scopus 로고
    • Physical interactions between ABA response loci of Arabidopsis
    • Nakamura, S., Lynch, T.J., and Finkelstein, R.R. (2001). Physical interactions between ABA response loci of Arabidopsis. Plant J. 26, 627-635.
    • (2001) Plant J. , vol.26 , pp. 627-635
    • Nakamura, S.1    Lynch, T.J.2    Finkelstein, R.R.3
  • 26
    • 0027383637 scopus 로고
    • 1H NMR
    • 1H NMR. Proteins 17, 297-309.
    • (1993) Proteins , vol.17 , pp. 297-309
    • Nilges, M.1
  • 27
    • 0023732144 scopus 로고
    • Determination of the three-dimensional structures of proteins from inter-proton distance data by dynamic simulated annealing from a random array of atoms
    • Nilges, M., Clore, G.M., and Gronenborn, A.M. (1988). Determination of the three-dimensional structures of proteins from inter-proton distance data by dynamic simulated annealing from a random array of atoms. FEBS Lett. 239, 129-136.
    • (1988) FEBS Lett. , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 28
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo, C.O., and Sauer, R.T. (1992). Transcription factors: Structural families and principles of DNA recognition. Annu. Rev. Biochem. 61, 1053-1095.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.O.1    Sauer, R.T.2
  • 29
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C.N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995). How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 30
    • 0033582491 scopus 로고    scopus 로고
    • Regions of endonuclease EcoRII involved in DNA target recognition identified by membrane-bound peptide repertoires
    • Reuter, M., Shneider-Mergener, J., Kupper, D., Meisel, A., Mackeldanz, P., Krünger, D.H., and Schroeder, C. (1999). Regions of endonuclease EcoRII involved in DNA target recognition identified by membrane-bound peptide repertoires. J. Biol. Cnem. 274, 5213-5221.
    • (1999) J. Biol. Cnem. , vol.274 , pp. 5213-5221
    • Reuter, M.1    Shneider-Mergener, J.2    Kupper, D.3    Meisel, A.4    Mackeldanz, P.5    Krünger, D.H.6    Schroeder, C.7
  • 31
    • 0034671865 scopus 로고    scopus 로고
    • Arabidopsis transcription factors: Genome-wide comparative analysis among eukaryotes
    • Riechmann, J.L., et al. (2000). Arabidopsis transcription factors: Genome-wide comparative analysis among eukaryotes. Science 290, 2105-2110.
    • (2000) Science , vol.290 , pp. 2105-2110
    • Riechmann, J.L.1
  • 32
    • 0030566854 scopus 로고    scopus 로고
    • Kinetics of binding of Antp homeodomain to DNA analyzed by measurements of surface plasmon resonance
    • Seimiya, M., and Kurosawa, Y. (1996). Kinetics of binding of Antp homeodomain to DNA analyzed by measurements of surface plasmon resonance. FEBS Lett. 398, 279-284.
    • (1996) FEBS Lett. , vol.398 , pp. 279-284
    • Seimiya, M.1    Kurosawa, Y.2
  • 33
    • 20244377471 scopus 로고    scopus 로고
    • Functional annotation of a full-length Arabidopsis cDNA collection
    • Seki, M., et al. (2002). Functional annotation of a full-length Arabidopsis cDNA collection. Science 296, 141-145.
    • (2002) Science , vol.296 , pp. 141-145
    • Seki, M.1
  • 34
    • 2642713363 scopus 로고    scopus 로고
    • The conserved B3 domain of VIVIPAROUS1 has a cooperative DNA binding activity
    • Suzuki, M., Kao, C.Y., and McCarty, D.R. (1997). The conserved B3 domain of VIVIPAROUS1 has a cooperative DNA binding activity. Plant Cell 9, 799-807.
    • (1997) Plant Cell , vol.9 , pp. 799-807
    • Suzuki, M.1    Kao, C.Y.2    McCarty, D.R.3
  • 35
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F., and Higgins, D.G. (1997). The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 36
    • 0037329943 scopus 로고    scopus 로고
    • The roles of auxin response factor domains in auxin-responsive transcription
    • Tiwari, S.B., Hagen, G., and Guilfoyle, T. (2003). The roles of auxin response factor domains in auxin-responsive transcription. Plant Cell 15, 533-543.
    • (2003) Plant Cell , vol.15 , pp. 533-543
    • Tiwari, S.B.1    Hagen, G.2    Guilfoyle, T.3
  • 37
    • 0030796237 scopus 로고    scopus 로고
    • ARF1, a transcription factor that binds to auxin response elements
    • Ulmasov, T., Hagen, G., and Guifoyle, T.J. (1997). ARF1, a transcription factor that binds to auxin response elements. Science 276, 1865-1868.
    • (1997) Science , vol.276 , pp. 1865-1868
    • Ulmasov, T.1    Hagen, G.2    Guifoyle, T.J.3
  • 38
    • 0033180359 scopus 로고    scopus 로고
    • Dimerization and DNA binding of auxin response factors
    • Ulmasov, T., Hagen, G., and Guifoyle, T.J. (1999). Dimerization and DNA binding of auxin response factors. Plant J. 19, 309-319.
    • (1999) Plant J. , vol.19 , pp. 309-319
    • Ulmasov, T.1    Hagen, G.2    Guifoyle, T.J.3
  • 39
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner, G., Braun, G., Havel, T.F., Schaumann, T., Go, N., and Wüthrich, K. (1987). Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196, 611-639.
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, G.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wüthrich, K.6
  • 40
    • 0032920469 scopus 로고    scopus 로고
    • NMR structure of the Tn916 integrase-DNA complex
    • Wojciak, J.M., Connolly, K.M., and Clubb, R.T. (1999). NMR structure of the Tn916 integrase-DNA complex. Nat. Struct. Biol. 6, 366-373.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 366-373
    • Wojciak, J.M.1    Connolly, K.M.2    Clubb, R.T.3
  • 42
    • 10744225497 scopus 로고    scopus 로고
    • A novel zinc-binding motif revealed by solution structures of DNA-binding domains of Arabidopsis SBP-family transcription factors
    • Yamasaki, K., et al. (2004). A novel zinc-binding motif revealed by solution structures of DNA-binding domains of Arabidopsis SBP-family transcription factors. J. Mol. Biol. 337, 49-63.
    • (2004) J. Mol. Biol. , vol.337 , pp. 49-63
    • Yamasaki, K.1
  • 43
    • 0033762813 scopus 로고    scopus 로고
    • Structural genomics projects in Japan
    • Yokoyama, S., et al. (2000). Structural genomics projects in Japan. Nat. Struct. Biol. 7 (suppl.), 943-945.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 943-945
    • Yokoyama, S.1
  • 44
    • 0345549459 scopus 로고    scopus 로고
    • Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold
    • Zhou, X.E., Wang, Y., Reuter, M., Mücke, M., Krüger, D.H., Meehan, E.J., and Chen, L. (2004). Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold. J. Mol. Biol. 335, 307-319.
    • (2004) J. Mol. Biol. , vol.335 , pp. 307-319
    • Zhou, X.E.1    Wang, Y.2    Reuter, M.3    Mücke, M.4    Krüger, D.H.5    Meehan, E.J.6    Chen, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.