Autoimmunity and effector recognition in Arabidopsis thaliana can be uncoupled by mutations in the RRS1-R immune receptor

Autoimmunity and effector recognition in Arabidopsis thaliana can be uncoupled by mutations in the RRS1-R immune receptor

© 2018 The Authors. New Phytologist © 2018 New Phytologist Trust.

Détails bibliographiques
Publié dans:The New phytologist. - 1984. - 222(2019), 2 vom: 15. Apr., Seite 954-965
Auteur principal: Newman, Toby E (Auteur)
Autres auteurs: Lee, Jungmin, Williams, Simon J, Choi, Sera, Halane, Morgan K, Zhou, Jun, Solomon, Peter, Kobe, Bostjan, Jones, Jonathan D G, Segonzac, Cécile, Sohn, Kee Hoon
Format: Article en ligne
Langue:English
Publié: 2019
Accès à la collection:The New phytologist
Sujets:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Toll/interleukin-1 receptor (TIR) domain autoimmunity immune receptor complex paired nucleotide-binding leucine-rich repeat (NLR) Amino Acids Arabidopsis Proteins Plant Proteins plus... RRS1 protein, Arabidopsis rps4 protein, plant
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520 |a Plant nucleotide-binding leucine-rich repeat (NLR) disease resistance proteins recognize specific pathogen effectors and activate a cellular defense program. In Arabidopsis thaliana (Arabidopsis), Resistance to Ralstonia solanacearum 1 (RRS1-R) and Resistance to Pseudomonas syringae 4 (RPS4) function together to recognize the unrelated bacterial effectors PopP2 and AvrRps4. In the plant cell nucleus, the RRS1-R/RPS4 complex binds to and signals the presence of AvrRps4 or PopP2. The exact mechanism underlying NLR signaling and immunity activation remains to be elucidated. Using genetic and biochemical approaches, we characterized the intragenic suppressors of sensitive to low humidity 1 (slh1), a temperature-sensitive autoimmune allele of RRS1-R. Our analyses identified five amino acid residues that contribute to RRS1-RSLH1 autoactivity. We investigated the role of these residues in the RRS1-R allele by genetic complementation, and found that C15 in the Toll/interleukin-1 receptor (TIR) domain and L816 in the LRR domain were also important for effector recognition. Further characterization of the intragenic suppressive mutations located in the RRS1-R TIR domain revealed differing requirements for RRS1-R/RPS4-dependent autoimmunity and effector-triggered immunity. Our results provide novel information about the mechanisms which, in turn, hold an NLR protein complex inactive and allow adequate activation in the presence of pathogens 
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650 4 |a Toll/interleukin-1 receptor (TIR) domain 
650 4 |a autoimmunity 
650 4 |a immune receptor complex 
650 4 |a paired nucleotide-binding leucine-rich repeat (NLR) 
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650 7 |a Arabidopsis Proteins  |2 NLM 
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700 1 |a Lee, Jungmin  |e verfasserin  |4 aut 
700 1 |a Williams, Simon J  |e verfasserin  |4 aut 
700 1 |a Choi, Sera  |e verfasserin  |4 aut 
700 1 |a Halane, Morgan K  |e verfasserin  |4 aut 
700 1 |a Zhou, Jun  |e verfasserin  |4 aut 
700 1 |a Solomon, Peter  |e verfasserin  |4 aut 
700 1 |a Kobe, Bostjan  |e verfasserin  |4 aut 
700 1 |a Jones, Jonathan D G  |e verfasserin  |4 aut 
700 1 |a Segonzac, Cécile  |e verfasserin  |4 aut 
700 1 |a Sohn, Kee Hoon  |e verfasserin  |4 aut 
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