Journal
EMBO JOURNAL
Volume 33, Issue 17, Pages 1941-1959Publisher
WILEY
DOI: 10.15252/embj.201487923
Keywords
Magnaporthe oryzae; pathogen recognition; plant immunity; resistance protein; rice
Categories
Funding
- program 'contrat jeune scientifique' of INRA
- Japanese Society for the Promotion of Science
- Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry, Japan
- Ministry of Education, Cultures, Sports and Technology, Japan [23113009]
- JSPS KAKENHI [24248004, 23580065]
- COSTAction SUSTAIN [FA1208]
- Grants-in-Aid for Scientific Research [23580065, 26450055, 26292027] Funding Source: KAKEN
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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.
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