The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance

Stella Césari, Hiroyuki Kanzaki, Tadashi Fujiwara, Maud Bernoux, Véronique Chalvon, Yoji Kawano, Ko Shimamoto, Peter Dodds, Ryohei Terauchi, Thomas Kroj

研究成果査読

247 被引用数 (Scopus)

抄録

Plant resistance proteins of the class of nucleotide-binding and leucine-rich repeat domain proteins (NB-LRRs) are immune sensors which recognize pathogen-derived molecules termed avirulence (AVR) proteins. We show that RGA4 and RGA5, two NB-LRRs from rice, interact functionally and physically to mediate resistance to the fungal pathogen Magnaporthe oryzae and accomplish different functions in AVR recognition. RGA4 triggers an AVR-independent cell death that is repressed in the presence of RGA5 in both rice protoplasts and Nicotiana benthamiana. Upon recognition of the pathogen effector AVR-Pia by direct binding to RGA5, repression is relieved and cell death occurs. RGA4 and RGA5 form homo- and hetero-complexes and interact through their coiled-coil domains. Localization studies in rice protoplast suggest that RGA4 and RGA5 localize to the cytosol. Upon recognition of AVR-Pia, neither RGA4 nor RGA5 is re-localized to the nucleus. These results establish a model for the interaction of hetero-pairs of NB-LRRs in plants: RGA4 mediates cell death activation, while RGA5 acts as a repressor of RGA4 and as an AVR receptor. Synopsis Plant microbial resistance is mediated by a pair of interacting immune sensors, RGA4 and RGA5. RGA4 mediates cell death but is repressed by RGA5. The repressor is neutralized by binding of pathogen-derived proteins to the dimer. Rice NB-LRR pair RGA4 and RGA5 interact through their CC domains and form homo- and hetero-complexes. RGA4 triggers effector-independent resistance responses that are repressed by RGA5. Recognition and physical binding of the fungal effector protein AVR-Pia by RGA5 relieves repression and activates RGA4-dependent resistance signaling. Plant microbial resistance is mediated by a pair of interacting immune sensors, RGA4 and RGA5. RGA4 mediates cell death but is repressed by RGA5. The repressor is neutralized by binding of pathogen-derived proteins to the dimer.

本文言語English
ページ(範囲)1941-1959
ページ数19
ジャーナルEMBO Journal
33
17
DOI
出版ステータスPublished - 9月 1 2014
外部発表はい

ASJC Scopus subject areas

  • 神経科学一般
  • 分子生物学
  • 生化学、遺伝学、分子生物学一般
  • 免疫学および微生物学一般

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