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

Adachi, Hiroaki, Contreras, Mauricio, Harant, Adeline, Wu, Chih-Hang, Derevnina, Lida, Sakai, Toshiyuki, Duggan, Cian, Moratto, Eleonora, Bozkurt, Tolga O, Maqbool, Abbas, Win, Joe and Kamoun, Sophien (2019) An N-terminal motif in NLR immune receptors is functionally conserved across distantly related plant species. eLife, 8. ISSN 2050-084X

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Abstract

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 a1 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.

Item Type: Article
Additional Information: © 2019, Adachi et al.
Faculty \ School:
Faculty of Science > School of Biological Sciences
Depositing User: LivePure Connector
Date Deposited: 03 Dec 2019 02:12
Last Modified: 30 Jun 2020 00:05
URI: https://ueaeprints.uea.ac.uk/id/eprint/73235
DOI: 10.7554/eLife.49956

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