The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance.
EMBO J
; 33(17): 1941-59, 2014 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-25024433
ABSTRACT
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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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Plantas
/
Oryza
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Magnaporthe
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Resistência à Doença
Idioma:
En
Revista:
EMBO J
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Austrália