Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity

Xinhua Sun, Dmitry Lapin, Joanna M. Feehan, Sara C. Stolze, Katharina Kramer, Joram A. Dongus, Jakub Rzemieniewski, Servane Blanvillain-Baufumé, Anne Harzen, Jaqueline Bautor, Paul Derbyshire, Frank L. H. Menke, Iris Finkemeier, Hirofumi Nakagami, Jonathan D. G. Jones () and Jane E. Parker ()
Additional contact information
Xinhua Sun: Max Planck Institute for Plant Breeding Research
Dmitry Lapin: Max Planck Institute for Plant Breeding Research
Joanna M. Feehan: University of East Anglia
Sara C. Stolze: Max Planck Institute for Plant Breeding Research
Katharina Kramer: Max Planck Institute for Plant Breeding Research
Joram A. Dongus: Max Planck Institute for Plant Breeding Research
Jakub Rzemieniewski: Max Planck Institute for Plant Breeding Research
Servane Blanvillain-Baufumé: Max Planck Institute for Plant Breeding Research
Anne Harzen: Max Planck Institute for Plant Breeding Research
Jaqueline Bautor: Max Planck Institute for Plant Breeding Research
Paul Derbyshire: University of East Anglia
Frank L. H. Menke: University of East Anglia
Iris Finkemeier: Max Planck Institute for Plant Breeding Research
Hirofumi Nakagami: Max Planck Institute for Plant Breeding Research
Jonathan D. G. Jones: University of East Anglia
Jane E. Parker: Max Planck Institute for Plant Breeding Research

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-021-23614-x

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