ArticleThe Plant cell2013
The rice resistance protein pair RGA4/RGA5 recognizes the Magnaporthe oryzae effectors AVR-Pia and AVR1-CO39 by direct binding.
Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 274 papers.
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Who cites it
274 citing papers in PubMed.
- Genome-wide prediction of cloned disease resistance homologues across the Oryza genus.The plant genome · 2026Article
- Comparative genome assemblies reveal distinct allelic and structural variation at blast resistance loci in rice CT21375-F4-4 and Moroberekan.The plant genome · 2026Article
- Pathogenicity and virulence of the blast fungusVirulence · 2026Review
- Mechanisms and balanced regulation of plant immunity.Nature reviews. Molecular cell biology · 2026Review
- Harnessing Natural Diversity and Rational Design for Enhanced Plant Immunity.Plant, cell & environment · 2026Review
- Upcycling Industrial Lignin Into Cationic Hydrogels With Potential for Sustainable Plant Protection.ChemSusChem · 2026Article
- Functional Dissection of the Turnip Crinkle Virus Coat Protein Links ATG8 Association to Autophagy-Associated Antiviral Regulation.Molecular plant pathology · 2026Article
- Whole Genome Sequencing of the Moruga Hill Rice (Biotech (Basel (Switzerland)) · 2026Article
- An HMA-like integrated domain in the wheat tandem kinase WTK4 recognises an RNase-like pathogen effector.Nature communications · 2026Article
- Two folds, many faces: The Magnaporthe oryzae MAX effector AVR-Pia targets novel rice HMA domain-containing proteins.PLoS pathogens · 2026Article
- A plant pathogen effector blocks stepwise assembly of a helper NLR resistosome.Science advances · 2026Article
- Engineering an Exo70 integrated domain of a barley NLR for improved blast resistance.The Plant cell · 2026Article
- Pan-NLRome analysis uncovers genetic diversity and evolutionary dynamics among rice, maize and sorghum.The plant genome · 2026Article
- GWAS and genomic prediction of crown rust resistance in the southern US elite oat (Avena sativa L.) germplasm.The plant genome · 2026Article
- Dual recognition of structurally unrelated mildew effectors underlies the broad-spectrum resistance of Pm3e in wheat.Nature communications · 2026Article
- Pathogenicity Analysis and Molecular Characterization of ThreeMicroorganisms · 2026Article
- Exploiting plant immune "switches" for resistance engineering.Stress biology · 2026Review
- An Auto-Activated NLR-Protein OsRGA3Plant biotechnology journal · 2026Article
- Fine mapping and candidate gene dissection of the wheat powdery mildew resistance gene PmPBDH.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026Article
- Mismatch screening in Nicotiana benthamiana to explore Pik-1/Pik-2 paired NLR platforms for receptor engineering.The New phytologist · 2026Article
214 more citing papers are in PubMed but not listed here.
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15 authors.
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No grant is acknowledged in the PubMed record.
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.
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