Structural and functional analysis of a plant resistance protein TIR Domain reveals interfaces for self-association, signaling, and autoregulation

Bemoux, Maud, Ve, Thomas, Williams, Simon, Warren, Christopher, Hatters, Danny, Valkov, Eugene, Zhang, Xiaoxiao, Ellis, Jeffrey G., Kobe, Bostjan and Dodds, Peter N. (2011) Structural and functional analysis of a plant resistance protein TIR Domain reveals interfaces for self-association, signaling, and autoregulation. Cell Host and Microbe, 9 3: 200-211. doi:10.1016/j.chom.2011.02.009


Author Bemoux, Maud
Ve, Thomas
Williams, Simon
Warren, Christopher
Hatters, Danny
Valkov, Eugene
Zhang, Xiaoxiao
Ellis, Jeffrey G.
Kobe, Bostjan
Dodds, Peter N.
Title Structural and functional analysis of a plant resistance protein TIR Domain reveals interfaces for self-association, signaling, and autoregulation
Journal name Cell Host and Microbe   Check publisher's open access policy
ISSN 1931-3128
1934-6069
Publication date 2011-03-01
Sub-type Article (original research)
DOI 10.1016/j.chom.2011.02.009
Volume 9
Issue 3
Start page 200
End page 211
Total pages 12
Place of publication Cambridge, MA, United States
Publisher Cell Press
Collection year 2012
Language eng
Abstract The Toll/interleukin-1 receptor (TIR) domain occurs in animal and plant immune receptors. In the animal Toll-like receptors, homodimerization of the intracellular TIR domain is required for initiation of signaling cascades leading to innate immunity. By contrast, the role of the TIR domain in cytoplasmic nucleotide-binding/leucine-rich repeat (NB-LRR) plant immune resistance proteins is poorly understood. L6 is a TIR-NB-LRR resistance protein from flax (Linum usitatissimum) that confers resistance to the flax rust phytopathogenic fungus (Melampsora lini). We determine the crystal structure of the L6 TIR domain and show that, although dispensable for pathogenic effector protein recognition, the TIR domain alone is both necessary and sufficient for L6 immune signaling. We demonstrate that the L6 TIR domain self-associates, most likely forming a homodimer. Analysis of the structure combined with site-directed mutagenesis suggests that self-association is a requirement for immune signaling and reveals distinct surface regions involved in self-association, signaling, and autoregulation.
Keyword For-Gene Specificity
Crystal-Structure
Innate Immunity
Macromolecular Crystallography
Avirulence Genes
Flax
Activation
Apoptosome
Receptor
Tobacco
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Available online 16 March 2011.

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
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