Agritrop
Home

The rice resistance protein pair RGA4/RGA5 recognizes the Magnaporthe oryzae effectors AVR-Pia and AVR1-CO39 by direct binding

Cesari Stella, Thilliez Gaëtan, Ribot Cécile, Chalvon Véronique, Michel Corinne, Jauneau Alain, Rivas Susana, Alaux Ludovic, Kanzaki Hiroyuki, Okuyama Yudai, Morel Jean-Benoit, Fournier Elisabeth, Tharreau Didier, Terauchi Ryohei, Kroj Thomas. 2013. The rice resistance protein pair RGA4/RGA5 recognizes the Magnaporthe oryzae effectors AVR-Pia and AVR1-CO39 by direct binding. Plant Cell, 25 (4) : pp. 1463-1481.

Journal article ; Article de revue à facteur d'impact
[img] Published version - Anglais
Access restricted to CIRAD agents
Use under authorization by the author or CIRAD.
document_569450.pdf

Télécharger (2MB)

Quartile : Outlier, Sujet : PLANT SCIENCES / Quartile : Outlier, Sujet : BIOCHEMISTRY & MOLECULAR BIOLOGY / Quartile : Q1, Sujet : CELL BIOLOGY

Abstract : Resistance (R) proteins recognize pathogen avirulence (Avr) proteins by direct or indirect binding and are multidomain proteins generally carrying a nucleotide binding (NB) and a leucine-rich repeat (LRR) domain. Two NB-LRR protein-coding genes from rice (Oryza sativa), RGA4 and RGA5, were found to be required for the recognition of the Magnaporthe oryzae effector AVR1-CO39. RGA4 and RGA5 also mediate recognition of the unrelated M. oryzae effector AVR-Pia, indicating that the corresponding R proteins possess dual recognition specificity. For RGA5, two alternative transcripts, RGA5-A and RGA5- B, were identified. Genetic analysis showed that only RGA5-A confers resistance, while RGA5-B is inactive. Yeast two-hybrid, coimmunoprecipitation, and fluorescence resonance energy transfer-fluorescence lifetime imaging experiments revealed direct binding of AVR-Pia and AVR1-CO39 to RGA5-A, providing evidence for the recognition of multiple Avr proteins by direct binding to a single R protein. Direct binding seems to be required for resistance as an inactive AVR-Pia allele did not bind RGA5-A. A small Avr interaction domain with homology to the Avr recognition domain in the rice R protein Pik-1 was identified in the C terminus of RGA5-A. This reveals a mode of Avr protein recognition through direct binding to a novel, non-LRR interaction domain. (Résumé d'auteur)

Mots-clés Agrovoc : Oryza sativa, Magnaporthe, Résistance aux maladies, Résistance génétique, mécanisme de défense, Protéine, Phylogénie

Mots-clés complémentaires : Magnaporthe oryzae

Classification Agris : F30 - Plant genetics and breeding
H20 - Plant diseases

Champ stratégique Cirad : Axe 1 (2005-2013) - Intensification écologique

Auteurs et affiliations

  • Cesari Stella, INRA (FRA)
  • Thilliez Gaëtan, INRA (FRA)
  • Ribot Cécile, INRA (FRA)
  • Chalvon Véronique, INRA (FRA)
  • Michel Corinne, INRA (FRA)
  • Jauneau Alain, CNRS (FRA)
  • Rivas Susana, INRA (FRA)
  • Alaux Ludovic, INRA (FRA)
  • Kanzaki Hiroyuki, IBRC (JPN)
  • Okuyama Yudai, IBRC (JPN)
  • Morel Jean-Benoit, INRA (FRA)
  • Fournier Elisabeth, INRA (FRA)
  • Tharreau Didier, CIRAD-BIOS-UMR BGPI (FRA) ORCID: 0000-0003-3961-6120
  • Terauchi Ryohei, IBRC (JPN)
  • Kroj Thomas, INRA (FRA)

Source : Cirad - Agritrop (https://agritrop.cirad.fr/569450/)

View Item (staff only) View Item (staff only)

[ Page générée et mise en cache le 2021-01-26 ]