Paired plant immune CHS3-CSA1 receptor alleles form distinct hetero-oligomeric complexes

• 成果类型: Article
• 署名作者: Yang, Yu; Furzer, Oliver J.; Fensterle, Eleanor P.; Lin, Shu; Zheng, Zhiyu; Kim, Nak Hyun; Wan, Li; Dangl, Jeffery L.
• 署名单位: University of North Carolina; University of North Carolina Chapel Hill; University of North Carolina; University of North Carolina Chapel Hill; Howard Hughes Medical Institute; Chinese Academy of Sciences; Center for Excellence in Molecular Plant Sciences, CAS
• 刊物名称: SCIENCE
• ISSN/ISSBN: 0036-9616
• DOI: 10.1126/science.adk3468
• 发表日期: 2024-02-16
• 关键词: cell-death; tir domains; resistosome; perception; activation; EVOLUTION; proteins; genes; nlrs

摘要

Plant intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) analyzed to date oligomerize and form resistosomes upon activation to initiate immune responses. Some NLRs are encoded in tightly linked co-regulated head-to-head genes whose products function together as pairs. We uncover the oligomerization requirements for different Arabidopsis paired CHS3-CSA1 alleles. These pairs form resting-state heterodimers that oligomerize into complexes distinct from NLRs analyzed previously. Oligomerization requires both conserved and allele-specific features of the respective CHS3 and CSA1 Toll-like interleukin-1 receptor (TIR) domains. The receptor kinases BAK1 and BIRs inhibit CHS3-CSA1 pair oligomerization to maintain the CHS3-CSA1 heterodimer in an inactive state. Our study reveals that paired NLRs hetero-oligomerize and likely form a distinctive dimer of heterodimers and that structural heterogeneity is expected even among alleles of closely related paired NLRs.