Sun, Xinhua, Lapin, Dmitry, Feehan, Joanna, Stolze, Sara C., Kramer, Katharina, Dongus, Joram A., Rzemieniewski, Jakub, Blanvillain-Baufumé, Servane, Harzen, Anne, Bautor, Jaqueline, Derbyshire, Paul, Menke, Frank ORCID: https://orcid.org/0000-0003-2490-4824, Finkemeier, Iris, Nakagami, Hirofumi, Jones, Jonathan D. G. and Parker, Jane E. (2021) Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity. Nature Communications, 12. ISSN 2041-1723
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Abstract
Plants utilise intracellular nucleotide-binding, leucine-rich repeat (NLR) immune receptors to detect pathogen effectors and activate local and systemic defence. NRG1 and ADR1 “helper” NLRs (RNLs) cooperate with enhanced disease susceptibility 1 (EDS1), senescence-associated gene 101 (SAG101) and phytoalexin-deficient 4 (PAD4) lipase-like proteins to mediate signalling from TIR domain NLR receptors (TNLs). The mechanism of RNL/EDS1 family protein cooperation is not understood. Here, we present genetic and molecular evidence for exclusive EDS1/SAG101/NRG1 and EDS1/PAD4/ADR1 co-functions in TNL immunity. Using immunoprecipitation and mass spectrometry, we show effector recognition-dependent interaction of NRG1 with EDS1 and SAG101, but not PAD4. An EDS1-SAG101 complex interacts with NRG1, and EDS1-PAD4 with ADR1, in an immune-activated state. NRG1 requires an intact nucleotide-binding P-loop motif, and EDS1 a functional EP domain and its partner SAG101, for induced association and immunity. Thus, two distinct modules (NRG1/EDS1/SAG101 and ADR1/EDS1/PAD4) mediate TNL receptor defence signalling.
Item Type: | Article |
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Faculty \ School: | Faculty of Science > The Sainsbury Laboratory Faculty of Science > School of Biological Sciences |
UEA Research Groups: | Faculty of Science > Research Groups > Plant Sciences |
Related URLs: | |
Depositing User: | LivePure Connector |
Date Deposited: | 05 Mar 2021 00:22 |
Last Modified: | 22 Oct 2022 10:30 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/79369 |
DOI: | 10.1038/s41467-021-23614-x |
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