An N-terminal motif in NLR immune receptors is functionally conserved across distantly related plant species

被引:157
作者
Adachi, Hiroaki [1 ]
Contreras, Mauricio P. [1 ]
Harant, Adeline [1 ]
Wu, Chih-hang [1 ]
Derevnina, Lida [1 ]
Sakai, Toshiyuki [1 ]
Duggan, Cian [2 ]
Moratto, Eleonora [2 ]
Bozkurt, Tolga O. [2 ]
Maqbool, Abbas [1 ]
Win, Joe [1 ]
Kamoun, Sophien [1 ]
机构
[1] Univ East Anglia, Sainsbury Lab, Norwich Res Pk, Norwich, Norfolk, England
[2] Imperial Coll London, Dept Life Sci, London, England
基金
欧洲研究理事会; 英国生物技术与生命科学研究理事会;
关键词
PHYTOPHTHORA-INFESTANS; COILED-COIL; RESISTANCE; REVEALS; POTATO; ACTIVATION; EFFECTOR; DEFENSE; DOMAINS; DEATH;
D O I
10.7554/eLife.49956
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The molecular codes underpinning the functions of plant NLR immune receptors are poorly understood. We used in vitro Mu transposition to generate a random truncation library and identify the minimal functional region of NLRs. We applied this method to NRC4-a helper NLR that functions with multiple sensor NLRs within a Solanaceae receptor network. This revealed that the NRC4 N-terminal 29 amino acids are sufficient to induce hypersensitive cell death. This region is defined by the consensus MADAxVSFxVxKLxxLLxxEx (MADA motif) that is conserved at the N-termini of NRC family proteins and similar to 20% of coiled-coil (CC)-type plant NLRs. The MADA motif matches the N-terminal alpha 1 helix of Arabidopsis NLR protein ZAR1, which undergoes a conformational switch during resistosome activation. Immunoassays revealed that the MADA motif is functionally conserved across NLRs from distantly related plant species. NRC-dependent sensor NLRs lack MADA sequences indicating that this motif has degenerated in sensor NLRs over evolutionary time.
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页数:31
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