Yamasaki Kazuhiko, Kigawa Takanori, Inoue Makoto, Tateno Masaru, Yamasaki Tomoko, Yabuki Takashi, Aoki Masaaki, Seki Eiko, Matsuda Takayoshi, Tomo Yasuko, Hayami Nobuhiro, Terada Takaho, Shirouzu Mikako, Osanai Takashi, Tanaka Akiko, Seki Motoaki, Shinozaki Kazuo, Yokoyama Shigeyuki
Age Dimension Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba 305-8566, Japan.
Plant Cell. 2004 Dec;16(12):3448-59. doi: 10.1105/tpc.104.026112. Epub 2004 Nov 17.
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.
B3 DNA结合结构域存在于多种植物特异性转录因子中，包括参与生长素调节和脱落酸调节转录的因子。在此，我们报道了拟南芥冷响应转录因子RAV1的B3结构域的核磁共振溶液结构。该结构由一个七链开放β桶和位于桶两端的两个α螺旋组成，与限制性内切酶EcoRII的非催化DNA结合结构域的结构显著相似。核磁共振滴定实验揭示了一个DNA识别界面，使我们能够提出蛋白质-DNA复合物的结构模型。与DNA接触的残基的位置也可能与EcoRII DNA结合结构域的相似。
