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

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 t...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2024-02, Vol.383 (6684), p.eadk3468-eadk3468
Main Authors: Yang, Yu, Furzer, Oliver J, Fensterle, Eleanor P, Lin, Shu, Zheng, Zhiyu, Kim, Nak Hyun, Wan, Li, Dangl, Jeffery L
Format: Article
Language:English
Subjects:
Adenine
Alleles
Binding
Cell death
Chromosomes
Damage patterns
Dimerization
Down-regulation
Feedback (Response)
Gene families
Genetic code
Heterogeneity
Immune response
Immune system
Innate immunity
Interleukin 1
Intracellular
Kinases
Leucine
NAD
Nicotinamide
Nicotinamide adenine dinucleotide
Nlr protein
Nucleotides
Oligomerization
Oligomers
Pathogens
Phylogeny
Plant immunity
Proteins
Receptors
Self-association
Sensors
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 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.
ISSN:0036-8075
1095-9203
1095-9203
DOI:10.1126/science.adk3468