Nucleic Acids Research Advance Access originally published online on January 30, 2007
Nucleic Acids Research 2007 35(4):1145-1154; doi:10.1093/nar/gkm001
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Nucleic Acids Research, 2007, Vol. 35, No. 4 1145-1154
© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Structural Biology |
DNA binding mechanism revealed by high resolution crystal structure of Arabidopsis thaliana WRKY1 protein
1The National Laboratory of Protein Engineering and Plant Genetic Engineering, Peking University, Beijing 100871, P.R. China, 2Peking-Yale Joint Center for Plant Molecular Genetics and Agrobiotechnology, Beijing 100871, P.R. China and 3College of Chemistry and Chemical Engineering, Peking University, Beijing 100871, P.R. China
*To whom correspondence should be addressed: Tel: +86 10 6275 9743; Fax: +86 10 6276 5669; Email: su-xd{at}pku.edu.cn; Yi Li. Tel: +86 10 6275 9690; Fax: +86 10 6275 4427; E-mail: liyi{at}pku.edu.cn
Received August 11, 2006. Revised December 20, 2006. Accepted December 22, 2006.
WRKY proteins, defined by the conserved WRKYGQK sequence, are comprised of a large superfamily of transcription factors identified specifically from the plant kingdom. This superfamily plays important roles in plant disease resistance, abiotic stress, senescence as well as in some developmental processes. In this study, the Arabidopsis WRKY1 was shown to be involved in the salicylic acid signaling pathway and partially dependent on NPR1; a C-terminal domain of WRKY1, AtWRKY1-C, was constructed for structural studies. Previous investigations showed that DNA binding of the WRKY proteins was localized at the WRKY domains and these domains may define novel zinc-binding motifs. The crystal structure of the AtWRKY1-C determined at 1.6 Å resolution has revealed that this domain is composed of a globular structure with five ß strands, forming an antiparallel ß-sheet. A novel zinc-binding site is situated at one end of the ß-sheet, between strands ß4 and ß5. Based on this high-resolution crystal structure and site-directed mutagenesis, we have defined and confirmed that the DNA-binding residues of AtWRKY1-C are located at ß2 and ß3 strands. These results provided us with structural information to understand the mechanism of transcriptional control and signal transduction events of the WRKY proteins.
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.
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