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Updated: Jul 3, 2025

In Vitro Reconstitution of Light-harvesting Complexes of Plants and Green Algae
Published on: October 10, 2014
Paired plant immune CHS3-CSA1 receptor alleles form distinct hetero-oligomeric complexes
Yu Yang1,2, Oliver J Furzer1,2, Eleanor P Fensterle1
1Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Abstract:
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.
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