A novel role for the TIR domain in association with pathogen-derived elicitors

Plant innate immunity is mediated by Resistance (R) proteins, which bear a striking resemblance to animal molecules of similar function. Tobacco N is a TIR-NB-LRR R gene that confers resistance to Tobacco mosaic virus, specifically the p50 helicase domain. An intriguing question is how plant R prote...

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Bibliographic Details
Published in:PLoS biology 2007-03, Vol.5 (3), p.e68-e68
Main Authors: Burch-Smith, Tessa M, Schiff, Michael, Caplan, Jeffrey L, Tsao, Jeffrey, Czymmek, Kirk, Dinesh-Kumar, Savithramma P
Format: Article
Language:English
Subjects:
Agricultural production
Amino Acid Sequence
Amino acids
Binding sites
Cytokines
Genes
Genetic aspects
Hypotheses
Immunity, Innate
Natural immunity
Nematodes
Plant Proteins - physiology
Plant resistance
Plants - immunology
Plants - virology
Polymerase Chain Reaction
Proteins
Tobacco
Tobacco (Plant)
Tobacco mosaic virus
Tobacco Mosaic Virus - pathogenicity
Virulence
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Summary:Plant innate immunity is mediated by Resistance (R) proteins, which bear a striking resemblance to animal molecules of similar function. Tobacco N is a TIR-NB-LRR R gene that confers resistance to Tobacco mosaic virus, specifically the p50 helicase domain. An intriguing question is how plant R proteins recognize the presence of pathogen-derived Avirulence (Avr) elicitor proteins. We have used biochemical cell fraction and immunoprecipitation in addition to confocal fluorescence microscopy of living tissue to examine the association between N and p50. Surprisingly, both N and p50 are cytoplasmic and nuclear proteins, and N's nuclear localization is required for its function. We also demonstrate an in planta association between N and p50. Further, we show that N's TIR domain is critical for this association, and indeed, it alone can associate with p50. Our results differ from current models for plant innate immunity that propose detection is mediated solely through the LRR domains of these molecules. The data we present support an intricate process of pathogen elicitor recognition by R proteins involving multiple subcellular compartments and the formation of multiple protein complexes.
ISSN:1545-7885
1544-9173
1545-7885
DOI:10.1371/journal.pbio.0050068