Mar 17, 2011 · In this study, we used the L6 protein as a model to characterize plant TIR domain signaling activity and mode of action. Mutational analysis showed that the TIR domain is dispensable for AvrL567 recognition but is required for induction of defense responses.

NOD-like receptors (NLRs) are central components of the plant immune system. L6 is a Toll/interleukin-1 receptor (TIR) domain-containing NLR from flax (Linum usitatissimum) conferring immunity to the flax rust fungus.

Dec 7, 2016 · Based on the protein structures of RPS4 TIR and L6 TIR (Bernoux et al., 2011; Williams et al., 2014), the TIR domain is predicted to be located between residues 20 and 188 (Figure 1A).

Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 from Arabidopsis.

In this study, we used the L6 protein as a model to characterize plant TIR domain signaling activity and mode of action. Muta-tional analysis showed that the TIR domain is dispensable for AvrL567 recognition but is required for induction of defense responses.

Feb 1, 2011 · In this study, the crystallization, X-ray diffraction analysis and preliminary structure determination of the TIR domain from the flax resistance protein L6 (L6TIR) are reported. Plate-like crystals of L6TIR were obtained using PEG 200 as a …

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 ...

Sep 25, 2010 · 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 ...

Mutations that perturb either the αD/αE or αA/αE interface of the SNC1 TIR, L6 TIR, or RPS4 TIR abrogate this HR, and also appear to attenuate TIR–TIR interactions in solution (although these interactions are weak and transient in the wild-type proteins).

May 20, 2022 · Here, we show that plant TIR proteins, besides being NADases, act as 2′,3′-cAMP/cGMP synthetases by hydrolyzing RNA/DNA. Structural data show that a TIR domain adopts distinct oligomers with mutually exclusive NADase and synthetase activity.