Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thaliana

Wan, Li, Zhang, Xiaoxiao, Williams, Simon J., Ve, Thomas, Bernoux, Maud, Sohn, Kee Hoon, Jones, Jonathan D. G., Dodds, Peter N. and Kobe, Bostjan (2013) Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thaliana. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69 11: 1275-1280. doi:10.1107/S1744309113026614

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Author Wan, Li
Zhang, Xiaoxiao
Williams, Simon J.
Ve, Thomas
Bernoux, Maud
Sohn, Kee Hoon
Jones, Jonathan D. G.
Dodds, Peter N.
Kobe, Bostjan
Title Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thaliana
Formatted title
Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thaliana
Journal name Acta Crystallographica Section F: Structural Biology and Crystallization Communications   Check publisher's open access policy
ISSN 1744-3091
Publication date 2013-11-01
Year available 2013
Sub-type Article (original research)
DOI 10.1107/S1744309113026614
Open Access Status File (Publisher version)
Volume 69
Issue 11
Start page 1275
End page 1280
Total pages 6
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell Publishing
Language eng
Formatted abstract
The Toll/interleukin-1 receptor (TIR) domain is a protein-protein interaction domain that is found in both animal and plant immune receptors. The N-­terminal TIR domain from the nucleotide-binding (NB)-leucine-rich repeat (LRR) class of plant disease-resistance (R) proteins has been shown to play an important role in defence signalling. Recently, the crystal structure of the TIR domain from flax R protein L6 was determined and this structure, combined with functional studies, demonstrated that TIR-domain homodimerization is a requirement for function of the R protein L6. To advance the molecular understanding of the function of TIR domains in R-protein signalling, the protein expression, purification, crystallization and X-ray diffraction analyses of the TIR domains of the Arabidopsis thaliana R proteins RPS4 (resistance to Pseudomonas syringae 4) and RRS1 (resistance to Ralstonia solanacearum 1) and the resistance-like protein SNC1 (suppressor of npr1-1, constitutive 1) are reported here. RPS4 and RRS1 function cooperatively as a dual resistance-protein system that prevents infection by three distinct pathogens. SNC1 is implicated in resistance pathways in Arabidopsis and is believed to be involved in transcriptional regulation through its interaction with the transcriptional corepressor TPR1 (Topless-related 1). The TIR domains of all three proteins have successfully been expressed and purified as soluble proteins in Escherichia coli. Plate-like crystals of the RPS4 TIR domain were obtained using PEG 3350 as a precipitant; they diffracted X-rays to 2.05 Å resolution, had the symmetry of space group P1 and analysis of the Matthews coefficient suggested that there were four molecules per asymmetric unit. Tetragonal crystals of the RRS1 TIR domain were obtained using ammonium sulfate as a precipitant; they diffracted X-rays to 1.75 Å resolution, had the symmetry of space group P41212 or P43212 and were most likely to contain one molecule per asymmetric unit. Crystals of the SNC1 TIR domain were obtained using PEG 3350 as a precipitant; they diffracted X-rays to 2.20 Å resolution and had the symmetry of space group P41212 or P43212, with two molecules predicted per asymmetric unit. These results provide a good foundation to advance the molecular and structural understanding of the function of the TIR domain in plant innate immunity.
Keyword Plant innate immunity
Resistance proteins
Toll/interleukin-1 receptor domain
RPS4
RRS1
SNC1
Hypersensitive response
Arabidopsis thaliana.
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID DP120100685
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2014 Collection
School of Chemistry and Molecular Biosciences
 
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Created: Wed, 13 Nov 2013, 00:35:55 EST by Mrs Louise Nimwegen on behalf of School of Chemistry & Molecular Biosciences