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SRFR1 negatively regulates plant NB-LRR resistance protein accumulation to prevent autoimmunity.
Li, Yingzhong; Li, Shuxin; Bi, Dongling; Cheng, Yu Ti; Li, Xin; Zhang, Yuelin.
Afiliación
  • Li Y; National Institute of Biological Sciences, Zhongguancun Life Science Park, Beijing, People's Republic of China.
PLoS Pathog ; 6(9): e1001111, 2010 Sep 16.
Article en En | MEDLINE | ID: mdl-20862316
ABSTRACT
Plant defense responses need to be tightly regulated to prevent auto-immunity, which is detrimental to growth and development. To identify negative regulators of Resistance (R) protein-mediated resistance, we screened for mutants with constitutive defense responses in the npr1-1 background. Map-based cloning revealed that one of the mutant genes encodes a conserved TPR domain-containing protein previously known as SRFR1 (SUPPRESSOR OF rps4-RLD). The constitutive defense responses in the srfr1 mutants in Col-0 background are suppressed by mutations in SNC1, which encodes a TIR-NB-LRR (Toll Interleukin1 Receptor-Nucleotide Binding-Leu-Rich Repeat) R protein. Yeast two-hybrid screens identified SGT1a and SGT1b as interacting proteins of SRFR1. The interactions between SGT1 and SRFR1 were further confirmed by co-immunoprecipitation analysis. In srfr1 mutants, levels of multiple NB-LRR R proteins including SNC1, RPS2 and RPS4 are increased. Increased accumulation of SNC1 is also observed in the sgt1b mutant. Our data suggest that SRFR1 functions together with SGT1 to negatively regulate R protein accumulation, which is required for preventing auto-activation of plant immunity.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Plantas / Arabidopsis / Proteínas de Arabidopsis / Inmunidad de la Planta / Glucosiltransferasas Idioma: En Revista: PLoS Pathog Año: 2010 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas de Plantas / Arabidopsis / Proteínas de Arabidopsis / Inmunidad de la Planta / Glucosiltransferasas Idioma: En Revista: PLoS Pathog Año: 2010 Tipo del documento: Article