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Variation in plant Toll/Interleukin-1 receptor domain protein dependence on ENHANCED DISEASE SUSCEPTIBILITY 1
Authors:Oliver Johanndrees,Erin L Baggs,Charles Uhlmann,Federica Locci,Henriette L Lä  ß  le,Katharina Melkonian,Kiara Kä  ufer,Joram A Dongus,Hirofumi Nakagami,Ksenia V Krasileva,Jane E Parker,Dmitry Lapin
Affiliation:Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Cologne, Germany;Department of Plant and Microbial Biology, University of California Berkeley, Berkeley, California, USA;Earlham Institute, Norwich Research Park, Norwich, UK;Cluster of Excellence on Plant Sciences (CEPLAS), Düsseldorf, Germany;Department of Biology, Translational Plant Biology, Utrecht University, Utrecht, The Netherlands
Abstract:Toll/Interleukin-1 receptor (TIR) domains are integral to immune systems across all kingdoms. In plants, TIRs are present in nucleotide-binding leucine-rich repeat (NLR) immune receptors, NLR-like, and TIR-only proteins. Although TIR-NLR and TIR signaling in plants require the ENHANCED DISEASE SUSCEPTIBILITY 1 (EDS1) protein family, TIRs persist in species that have no EDS1 members. To assess whether particular TIR groups evolved with EDS1, we searched for TIR-EDS1 co-occurrence patterns. Using a large-scale phylogenetic analysis of TIR domains from 39 algal and land plant species, we identified 4 TIR families that are shared by several plant orders. One group occurred in TIR-NLRs of eudicots and another in TIR-NLRs across eudicots and magnoliids. Two further groups were more widespread. A conserved TIR-only group co-occurred with EDS1 and members of this group elicit EDS1-dependent cell death. In contrast, a maize (Zea mays) representative of TIR proteins with tetratricopeptide repeats was also present in species without EDS1 and induced EDS1-independent cell death. Our data provide a phylogeny-based plant TIR classification and identify TIRs that appear to have evolved with and are dependent on EDS1, while others have EDS1-independent activity.

Plant Toll/Interleukin-1 receptor domain proteins can use different mechanisms to induce cell death.
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