title: Solution structure of the B3 DNA binding domain of the Arabidopsis cold-responsive transcription factor RAV1.
abstract: The B3 DNA binding domain is shared amongst various plant-specific transcription factors, including factors involved in auxin-regulated and abscisic acid-regulated transcription. Herein, we report the NMR solution structure of the B3 domain of the Arabidopsis thaliana cold-responsive transcription factor RAV1. The structure consists of a seven-stranded open beta-barrel and two alpha-helices located at the ends of the barrel and is significantly similar to the structure of the noncatalytic DNA binding domain of the restriction enzyme EcoRII. An NMR titration experiment revealed a DNA recognition interface that enabled us to propose a structural model of the protein-DNA complex. The locations of the DNA-contacting residues are also likely to be similar to those of the EcoRII DNA binding domain.
authors.affiliation: Age Dimension Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba 305-8566, Japan. k-yamasaki@aist.go.jp
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Yamasaki
authors.forename: Takanori
authors.initials: T
authors.lastname: Kigawa
authors.forename: Makoto
authors.initials: M
authors.lastname: Inoue
authors.forename: Masaru
authors.initials: M
authors.lastname: Tateno
authors.forename: Tomoko
authors.initials: T
authors.lastname: Yamasaki
authors.forename: Takashi
authors.initials: T
authors.lastname: Yabuki
authors.forename: Masaaki
authors.initials: M
authors.lastname: Aoki
authors.forename: Eiko
authors.initials: E
authors.lastname: Seki
authors.forename: Takayoshi
authors.initials: T
authors.lastname: Matsuda
authors.forename: Yasuko
authors.initials: Y
authors.lastname: Tomo
authors.forename: Nobuhiro
authors.initials: N
authors.lastname: Hayami
authors.forename: Takaho
authors.initials: T
authors.lastname: Terada
authors.forename: Mikako
authors.initials: M
authors.lastname: Shirouzu
authors.forename: Takashi
authors.initials: T
authors.lastname: Osanai
authors.forename: Akiko
authors.initials: A
authors.lastname: Tanaka
authors.forename: Motoaki
authors.initials: M
authors.lastname: Seki
authors.forename: Kazuo
authors.initials: K
authors.lastname: Shinozaki
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: D000064:Acclimatization / Q000502:physiology; D000595:Amino Acid Sequence / Q000502:physiology; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites / Q000235:genetics; D003080:Cold Temperature; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015252:Deoxyribonucleases, Type II Site-Specific / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D008958:Models, Molecular; D008968:Molecular Conformation; D019906:Nuclear Magnetic Resonance, Biomolecular; D010802:Phylogeny; D017433:Protein Structure, Secondary / Q000502:physiology; D017434:Protein Structure, Tertiary / Q000235:genetics; D017386:Sequence Homology, Amino Acid
chemical_list: D029681:Arabidopsis Proteins; D004268:DNA-Binding Proteins; C117695:RAV1 protein, Arabidopsis; D004247:DNA; C046545:CCWGG-specific type II deoxyribonucleases; D015252:Deoxyribonucleases, Type II Site-Specific