Solution structure of the B3 DNA binding domain of the Arabidopsis cold-responsive transcription factor RAV1

被引：109

作者：

Yamasaki, K ^{[1
]}

Kigawa, T

Inoue, M

Tateno, M

Yamasaki, T

Yabuki, T

Aoki, M

Seki, E

Matsuda, T

Tomo, Y

Hayami, N

Terada, T

Shirouzu, M

Osanai, T

Tanaka, A

Motoaki, S

Shinozaki, K

Yokoyama, S

机构：

[1] Natl Inst Adv Ind Sci & Technol, Age Dimens Res Ctr, Tsukuba, Ibaraki 3058566, Japan

[2] RIKEN, Genom Sci Ctr, Prot Res Grp, Yokohama, Kanagawa 2300045, Japan

[3] Tokyo Inst Technol, Ctr Biol Resources & Informat, Yokohama, Kanagawa 2268501, Japan

[4] RIKEN, Tsukuba Inst, Lab Plant Mol Biol, Tsukuba, Ibaraki 3050074, Japan

[5] RIKEN, Genom Sci Ctr, Plant Funct Genom Res Grp, Yokohama, Kanagawa 2300045, Japan

[6] Univ Tsukuba, Inst Biol Sci, Tsukuba, Ibaraki 3058572, Japan

[7] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Tokyo 1130033, Japan

来源：

PLANT CELL | 2004年 / 16卷 / 12期

关键词：

D O I：

10.1105/tpc.104.026112

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 133 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.

引用

页码：3448 / 3459

页数：12

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