| Literature DB >> 34099661 |
Xinhua Sun1, Dmitry Lapin1,2, Joanna M Feehan3, Sara C Stolze4, Katharina Kramer4, Joram A Dongus1, Jakub Rzemieniewski1,5, Servane Blanvillain-Baufumé1, Anne Harzen4, Jaqueline Bautor1, Paul Derbyshire3, Frank L H Menke3, Iris Finkemeier4,6, Hirofumi Nakagami1,4, Jonathan D G Jones7, Jane E Parker8,9.
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.Entities:
Year: 2021 PMID： 34099661 DOI： 10.1038/s41467-021-23614-x
Source DB: PubMed Journal: Nat Commun ISSN： 2041-1723 Impact factor: 14.919