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Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity
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Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity
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Journal Article
Pathogen effector recognition-dependent association of NRG1 with EDS1 and SAG101 in TNL receptor immunity
2021
Overview
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.
For defence, plants deploy nucleotide binding, leucine-rich repeat (NLR) immune receptors to detect pathogens that signal via modular networks of downstream proteins. Here the authors report rapid induced association of non-interchangeable signalling pathway module components after NLR activation.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 38/44
/ 45/22
/ 45/29
/ 45/77
/ 82/1
/ 82/16
/ 82/58
/ 82/80
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Binding
/ Carboxylic Ester Hydrolases - chemistry
/ Carboxylic Ester Hydrolases - genetics
/ Carboxylic Ester Hydrolases - metabolism
/ DNA-Binding Proteins - chemistry
/ DNA-Binding Proteins - genetics
/ DNA-Binding Proteins - metabolism
/ Domains
/ Humanities and Social Sciences
/ Immunity
/ Leucine
/ Modules
/ Plant Diseases - microbiology
/ Plants, Genetically Modified
/ Proteins
/ Receptors, Immunologic - chemistry
/ Receptors, Immunologic - genetics
/ Receptors, Immunologic - metabolism
/ Science
