Three highly conserved hydrophobic residues in the predicted α2-helix of rice NLR protein Pit contribute to its localization and immune induction

Qiong Wang, Yuying Li, Ken ichi Kosami, Chaochao Liu, Jing Li, Dan Zhang, Daisuke Miki, Yoji Kawano

Research output: Contribution to journalArticlepeer-review

Abstract

Nucleotide-binding leucine-rich repeat (NLR) proteins work as crucial intracellular immune receptors. N-terminal domains of NLRs fall into two groups, coiled-coil (CC) and Toll-interleukin 1 receptor domains, which play critical roles in signal transduction and disease resistance. However, the activation mechanisms of NLRs, and how their N-termini function in immune induction, remain largely unknown. Here, we revealed that the CC domain of a rice NLR Pit contributes to self-association. The Pit CC domain possesses three conserved hydrophobic residues that are known to be involved in oligomer formation in two NLRs, barley MLA10 and Arabidopsis RPM1. Interestingly, the function of these residues in Pit differs from that in MLA10 and RPM1. Although three hydrophobic residues are important for Pit-induced disease resistance against rice blast fungus, they do not participate in self-association or binding to downstream signalling molecules. By homology modelling of Pit using the Arabidopsis ZAR1 structure, we tried to clarify the role of three conserved hydrophobic residues and found that they are located in the predicted α2-helix of the Pit CC domain and involved in the plasma membrane localization. Our findings provide novel insights for understanding the mechanisms of NLR activation as well as the relationship between subcellular localization and immune induction.

Original languageEnglish
Pages (from-to)1876-1890
Number of pages15
JournalPlant Cell and Environment
Volume45
Issue number6
DOIs
Publication statusPublished - Jun 2022

Keywords

  • effector-triggered immunity
  • plasma membrane localization
  • rice
  • self-association

ASJC Scopus subject areas

  • Physiology
  • Plant Science

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