Plant Cell Advance Online Publication
Published on November 17, 2004; 10.1105/tpc.104.026112
Received July 15, 2004
Accepted September 14, 2004
Solution Structure of the B3 DNA Binding Domain of the Arabidopsis Cold-Responsive Transcription Factor RAV1
Kazuhiko Yamasaki 1*, Takanori Kigawa 2, Makoto Inoue 2, Masaru Tateno 3, Tomoko Yamasaki 4, Takashi Yabuki 2, Masaaki Aoki 2, Eiko Seki 2, Takayoshi Matsuda 2, Yasuko Tomo 2, Nobuhiro Hayami 2, Takaho Terada 5, Mikako Shirouzu 5, Takashi Osanai 2, Akiko Tanaka 2, Motoaki Seki 6, Kazuo Shinozaki 7, and Shigeyuki Yokoyama 8
1 Age Dimension Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba 305-8566, Japan; Protein Research Group, RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan
2 Protein Research Group, RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan
3 Age Dimension Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba 305-8566, Japan; Center for Biological Resources and Informatics, Tokyo Institute of Technology, Yokohama 226-8501, Japan
4 Age Dimension Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba 305-8566, Japan
5 Protein Research Group, RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan; RIKEN Harima Institute at SPring8, Hyogo 679-5148, Japan
6 Laboratory of Plant Molecular Biology, RIKEN Tsukuba Institute, Tsukuba 305-0074, Japan; Plant Functional Genomics Research Group, RIKEN Genomic Sciences Center,Yokohama 230-0045, Japan
7 Laboratory of Plant Molecular Biology, RIKEN Tsukuba Institute, Tsukuba 305-0074, Japan; Plant Functional Genomics Research Group, RIKEN Genomic Sciences Center,Yokohama 230-0045, Japan; Institute of Biological Sciences, University of Tsukuba, Tsukuba 305-8572, Japan
8 Protein Research Group, RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan; RIKEN Harima Institute at SPring8, Hyogo 679-5148, Japan; Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan
* To whom correspondence should be addressed. E-mail: k-yamasaki{at}aist.go.jp.
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  -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.
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