Substrate-induced condensation activates plant TIR domain proteins

Wen Song, Li Liu, Dongli Yu, Hanna Bernardy, Jan Jirschitzka, Shijia Huang, Aolin Jia, Wictoria Jemielniak, Julia Acker, Henriette Laessle, Junli Wang, Qiaochu Shen, Weijie Chen, Pilong Li, Jane E. Parker, Zhifu Han, Paul Schulze-Lefert () and Jijie Chai ()
Additional contact information
Wen Song: China Agricultural University
Li Liu: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research
Dongli Yu: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research
Hanna Bernardy: University of Cologne
Jan Jirschitzka: University of Cologne
Shijia Huang: Westlake University, Institute of Biology, Westlake Institute for Advanced Study
Aolin Jia: Tsinghua University
Wictoria Jemielniak: University of Cologne
Julia Acker: University of Cologne
Henriette Laessle: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research
Junli Wang: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research
Qiaochu Shen: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research
Weijie Chen: Tsinghua University
Pilong Li: Tsinghua University
Jane E. Parker: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research
Zhifu Han: Westlake University, Institute of Biology, Westlake Institute for Advanced Study
Paul Schulze-Lefert: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research
Jijie Chai: Department of Plant Microbe Interactions, Max Planck Institute for Plant Breeding Research

Nature, 2024, vol. 627, issue 8005, 847-853

Abstract: Abstract Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors with an N-terminal Toll/interleukin-1 receptor (TIR) domain mediate recognition of strain-specific pathogen effectors, typically via their C-terminal ligand-sensing domains1. Effector binding enables TIR-encoded enzymatic activities that are required for TIR–NLR (TNL)-mediated immunity2,3. Many truncated TNL proteins lack effector-sensing domains but retain similar enzymatic and immune activities4,5. The mechanism underlying the activation of these TIR domain proteins remain unclear. Here we show that binding of the TIR substrates NAD+ and ATP induces phase separation of TIR domain proteins in vitro. A similar condensation occurs with a TIR domain protein expressed via its native promoter in response to pathogen inoculation in planta. The formation of TIR condensates is mediated by conserved self-association interfaces and a predicted intrinsically disordered loop region of TIRs. Mutations that disrupt TIR condensates impair the cell death activity of TIR domain proteins. Our data reveal phase separation as a mechanism for the activation of TIR domain proteins and provide insight into substrate-induced autonomous activation of TIR signalling to confer plant immunity.

Date: 2024
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DOI: 10.1038/s41586-024-07183-9

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