效应器
细胞生物学
生物
蛋白质结构域
血浆蛋白结合
受体
信号转导
先天免疫系统
化学
生物物理学
生物化学
基因
作者
Wen Song,Li Liu,Dongli Yu,Hanna Bernardy,Jan Jirschitzka,Shijia Huang,Aolin Jia,Wictoria Jemielniak,Julia Acker,Henriette Laessle,Junli Wang,Qin Shen,Weijie Chen,Pilong Li,Jane E. Parker,Zhifu Han,Paul Schulze‐Lefert,Jijie Chai
出处
期刊:Nature
[Springer Nature]
日期:2024-03-13
被引量:3
标识
DOI:10.1038/s41586-024-07183-9
摘要
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.
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