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

Author

Listed:
  • Xinhua Sun

    (Max Planck Institute for Plant Breeding Research)

  • Dmitry Lapin

    (Max Planck Institute for Plant Breeding Research
    Utrecht University)

  • 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
    Technical University of Munich)

  • 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
    University of Muenster)

  • Hirofumi Nakagami

    (Max Planck Institute for Plant Breeding Research
    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
    Cologne-Düsseldorf Cluster of Excellence on Plant Sciences (CEPLAS))

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.

Suggested Citation

  • 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 Derbyshir, 2021. "Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23614-x
    DOI: 10.1038/s41467-021-23614-x
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