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Plant Cell. 2019 Jul 16. pii: tpc.00118.2019. doi: 10.1105/tpc.19.00118. [Epub ahead of print]

A coevolved EDS1-SAG101-NRG1 module mediates cell death signaling by TIR-domain immune receptors.

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Max-Planck Institute for Plant Breeding Research CITY: Cologne POSTAL_CODE: 50829 Germany [DE].
University of Cologne CITY: Cologne Germany [DE].
Max-Planck Institute for Plant Breeding Research CITY: Cologne Germany [DE].
Michigan State University CITY: east lansing STATE: MICHIGAN POSTAL_CODE: 48823 United States Of America [US].
Max Planck Institute for Plant Breeding Research CITY: Cologne Germany [DE].
Max Planck Institute for Plant Breeding Research CITY: 50829 Koeln Germany [DE].
Wageningen University CITY: Wageningen Germany [DE].
Martin Luther University Halle-Wittenberg CITY: Halle POSTAL_CODE: 6120 Germany [DE].
Max-Planck-Institute for Plant Breeding Research CITY: D-50829 Cologne POSTAL_CODE: N/A Germany [DE]


Plant intracellular nucleotide-binding/leucine-rich repeat (NLR) immune receptors are activated by pathogen effectors to trigger host defenses and cell death. Toll-Interleukin1-receptor (TIR)-domain NLRs (TNLs) converge on the Enhanced Disease Susceptibility1 (EDS1) family of lipase-like proteins for all resistance outputs. In Arabidopsis TNL immunity, AtEDS1 heterodimers with Phytoalexin Deficient4 (AtPAD4) transcriptionally boost basal defense pathways. AtEDS1 uses the same surface to interact with PAD4-related Senescence-Associated Gene101 (AtSAG101), but the role of AtEDS1-AtSAG101 heterodimers was unclear. We show that AtEDS1-AtSAG101 function together with AtNRG1 coiled-coil domain helper NLRs as a coevolved TNL cell death signaling module. AtEDS1-AtSAG101-AtNRG1 cell death activity is transferable to the solanaceous species, Nicotiana benthamiana, and cannot be substituted by AtEDS1-AtPAD4 with AtNRG1 or AtEDS1-AtSAG101 with endogenous NbNRG1. Analysis of EDS1-family evolutionary rate variation and heterodimer structure-guided phenotyping of AtEDS1 variants or AtPAD4-AtSAG101 chimeras identify closely aligned ɑ-helical coil surfaces in the AtEDS1-AtSAG101 partner C-terminal domains that are necessary for TNL cell death signaling. Our data suggest that TNL-triggered cell death and pathogen growth restriction are determined by distinctive features of EDS1-SAG101 and EDS1-PAD4 complexes and that these signaling machineries coevolved with further components within plant species or clades to regulate downstream pathways in TNL immunity.

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