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DNA binding mechanism revealed by high resolution crystal structure of Arabidopsis thaliana WRKY1 protein

Duan, Ming-Rui; Nan, Jie LU ; Liang, Yu-He; Mao, Peng; Lu, Lu; Li, Lanfen; Wei, Chunhong; Lai, Luhua; Li, Yi and Su, Xiao-Dong LU (2007) In Nucleic Acids Research 35(4). p.54-1145
Abstract

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 A... (More)

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 A resolution has revealed that this domain is composed of a globular structure with five beta strands, forming an antiparallel beta-sheet. A novel zinc-binding site is situated at one end of the beta-sheet, between strands beta4 and beta5. 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 beta2 and beta3 strands. These results provided us with structural information to understand the mechanism of transcriptional control and signal transduction events of the WRKY proteins.

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Contribution to journal
publication status
published
keywords
Amino Acid Sequence, Arabidopsis Proteins, Binding Sites, Cell Nucleus, Conserved Sequence, Crystallography, X-Ray, DNA, DNA-Binding Proteins, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Binding, Salicylic Acid, Sequence Alignment, Signal Transduction, Transcription Factors, Zinc
in
Nucleic Acids Research
volume
35
issue
4
pages
10 pages
publisher
Oxford University Press
external identifiers
  • scopus:34047176925
ISSN
1362-4962
DOI
10.1093/nar/gkm001
language
English
LU publication?
yes
id
9e8cefde-9bbd-4e1e-b607-166db57008f8
date added to LUP
2016-09-07 22:54:17
date last changed
2017-10-22 05:18:57
@article{9e8cefde-9bbd-4e1e-b607-166db57008f8,
  abstract     = {<p>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 A resolution has revealed that this domain is composed of a globular structure with five beta strands, forming an antiparallel beta-sheet. A novel zinc-binding site is situated at one end of the beta-sheet, between strands beta4 and beta5. 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 beta2 and beta3 strands. These results provided us with structural information to understand the mechanism of transcriptional control and signal transduction events of the WRKY proteins.</p>},
  author       = {Duan, Ming-Rui and Nan, Jie and Liang, Yu-He and Mao, Peng and Lu, Lu and Li, Lanfen and Wei, Chunhong and Lai, Luhua and Li, Yi and Su, Xiao-Dong},
  issn         = {1362-4962},
  keyword      = {Amino Acid Sequence,Arabidopsis Proteins,Binding Sites,Cell Nucleus,Conserved Sequence,Crystallography, X-Ray,DNA,DNA-Binding Proteins,Hydrogen Bonding,Models, Molecular,Molecular Sequence Data,Mutagenesis, Site-Directed,Protein Binding,Salicylic Acid,Sequence Alignment,Signal Transduction,Transcription Factors,Zinc},
  language     = {eng},
  number       = {4},
  pages        = {54--1145},
  publisher    = {Oxford University Press},
  series       = {Nucleic Acids Research},
  title        = {DNA binding mechanism revealed by high resolution crystal structure of Arabidopsis thaliana WRKY1 protein},
  url          = {http://dx.doi.org/10.1093/nar/gkm001},
  volume       = {35},
  year         = {2007},
}