Solution Structure of the B3 DNA Binding Domain of the Arabidopsis Cold-Responsive Transcription Factor RAV1[W]-Reference-Cited by-同舟云学术

Solution Structure of the B3 DNA Binding Domain of the Arabidopsis Cold-Responsive Transcription Factor RAV1[W]

Published:2004-12-01 Issue:12 Volume:16 Page:3448-3459
ISSN:1532-298X
Container-title:The Plant Cell
language:en
Short-container-title:

Author:

Yamasaki Kazuhiko¹²,Kigawa Takanori²,Inoue Makoto²,Tateno Masaru¹³,Yamasaki Tomoko¹,Yabuki Takashi²,Aoki Masaaki²,Seki Eiko²,Matsuda Takayoshi²,Tomo Yasuko²,Hayami Nobuhiro²,Terada Takaho²⁴,Shirouzu Mikako²⁴,Osanai Takashi²,Tanaka Akiko²,Seki Motoaki⁵⁶,Shinozaki Kazuo⁵⁶⁷,Yokoyama Shigeyuki²⁴⁸

Affiliation:

1. Age Dimension Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba 305-8566, Japan

2. Protein Research Group, RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan

3. Center for Biological Resources and Informatics, Tokyo Institute of Technology, Yokohama 226-8501, Japan

4. RIKEN Harima Institute at SPring8, Hyogo 679-5148, Japan

5. Laboratory of Plant Molecular Biology, RIKEN Tsukuba Institute, Tsukuba 305-0074, Japan

6. Plant Functional Genomics Research Group, RIKEN Genomic Sciences Center,Yokohama 230-0045, Japan

7. Institute of Biological Sciences, University of Tsukuba, Tsukuba 305-8572, Japan

8. Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Tokyo 113-0033, Japan

Abstract

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 β-barrel and two α-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.

Publisher

Oxford University Press (OUP)

Subject

Cell Biology,Plant Science

Link

http://academic.oup.com/plcell/article-pdf/16/12/3448/36875792/plcell_v16_12_3448.pdf

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