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

By Hiroaki Adachi, Mauricio Contreras, Adeline Harant, Chih-hang Wu, Lida Derevnina, Toshiyuki Sakai, Cian Duggan, Eleonora Moratto, Tolga O Bozkurt, Abbas Maqbool, Joe Win, Sophien Kamoun

Posted 04 Jul 2019
bioRxiv DOI: 10.1101/693291 (published DOI: 10.7554/eLife.49956)

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 ~20% of coiled-coil (CC)-type plant NLRs. The MADA motif matches the N-terminal α1 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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