A Coevolved EDS1-SAG101-NRG1 Module Mediates Cell Death Signaling by TIR-Domain Immune Receptors
A Coevolved EDS1-SAG101-NRG1 Module Mediates Cell Death Signaling by TIR-Domain Immune Receptors
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DOI：
10.1105/tpc.19.00118
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发表时间：
2019-10-01
期刊：
影响因子：
11.6
通讯作者：
Parker, Jane E.
中科院分区：
文献类型：
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作者：
Lapin, Dmitry;Kovacova, Viera;Parker, Jane E.
植物核苷酸结合/富亮氨酸重复（NLR）免疫受体被病原体效应物激活，触发宿主防御和细胞死亡。toll -白细胞介素1受体结构域NLRs （TNLs）集中于增强疾病易感性1 （EDS1）家族脂酶样蛋白的所有抗性输出。在拟南芥（Arabidopsis thaliana） tnl介导的免疫中，具有植物alexin缺陷4 （AtPAD4）的AtEDS1异二聚体转录诱导基础防御。AtEDS1使用相同的表面与pad4相关的衰老相关基因101 （AtSAG101）相互作用，但AtEDS1-AtSAG101异源二聚体的作用尚不清楚。我们发现，AtEDS1-AtSAG101与N REQUIRED GENE1 （AtNRG1）线圈结构域辅助NLRs一起作为共同进化的TNL细胞死亡信号模块发挥作用。AtEDS1-AtSAG101-AtNRG1细胞死亡活性可转移到茄属植物benthamiana，并且不能被AtEDS1-AtPAD4与AtNRG1或AtEDS1-AtSAG101与内源性NbNRG1取代。分析eds1家族进化速率变异及异源二聚体结构引导下的AtEDS1变异与AtPAD4-AtSAG101嵌合体鉴定紧密一致。-螺旋线圈表面在AtEDS1-AtSAG101伴侣c端结构域中，这是重建TNL细胞死亡信号所必需的。我们的数据表明，TNL引发的细胞死亡和病原体生长限制是由EDS1-SAG101和EDS1-PAD4复合物的独特特征决定的，这些信号机制与植物物种或分支中的其他成分共同进化，调节TNL免疫的下游途径。
Plant nucleotide binding/leucine-rich repeat (NLR) immune receptors are activated by pathogen effectors to trigger host defenses and cell death. Toll-interleukin 1 receptor domain NLRs (TNLs) converge on the ENHANCED DISEASE SUSCEPTIBILITY1 (EDS1) family of lipase-like proteins for all resistance outputs. In Arabidopsis (Arabidopsis thaliana) TNL-mediated immunity, AtEDS1 heterodimers with PHYTOALEXIN DEFICIENT4 (AtPAD4) transcriptionally induced basal defenses. AtEDS1 uses the same surface to interact with PAD4-related SENESCENCE-ASSOCIATED GENE101 (AtSAG101), but the role of AtEDS1-AtSAG101 heterodimers remains unclear. We show that AtEDS1-AtSAG101 functions together with N REQUIRED GENE1 (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 and AtPAD4-AtSAG101 chimeras identify closely aligned.-helical coil surfaces in the AtEDS1-AtSAG101 partner C-terminal domains that are necessary for reconstituted 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 other components within plant species or clades to regulate downstream pathways in TNL immunity.