Author/Authors :
Inoue، Makoto نويسنده , , Yokoyama، Shigeyuki نويسنده , , Shinozaki، Kazuo نويسنده , , Seki، Motoaki نويسنده , , Yamasaki، Kazuhiko نويسنده , , Kigawa، Takanori نويسنده , , Tateno، Masaru نويسنده , , Yamasaki، Tomoko نويسنده , , Yabuki، Takashi نويسنده , , Aoki، Masaaki نويسنده , , Seki، Eiko نويسنده , , Matsuda، Takayoshi نويسنده , , Tomo، Yasuko نويسنده , , Hayami، Nobuhiro نويسنده , , Terada، Takaho نويسنده , , Shirouzu، Mikako نويسنده , , Osanai، Takashi نويسنده , , Tanaka، Akiko نويسنده ,
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 ?-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.
Keywords :
N deposition , Pine barrens , Ectomycorrhizae , Indicator species , Oligotrophic soils
