- Information
- Symbol: Pik-1
- MSU: None
- RAPdb: None
- Publication
- Development of DNA markers suitable for marker assisted selection of three Pi genes conferring resistance to multiple Pyricularia grisea pathotypes, 2004, Crop Science.
- The isolation and characterization of Pik, a rice blast resistance gene which emerged after rice domestication, 2011, New Phytol.
- Characterization of the rice blast resistance gene Pik cloned from Kanto51, 2011, Molecular Breeding.
- Genetic analysis of resistance/susceptibility in individual F3 families of rice against strains of Magnaporthe grisea containing different genes for avirulence, 1999, Euphytica.
- Genbank accession number
- Key message
- The rice blast resistance gene Pik, which is one of the five classical alleles located at the Pik locus on the long arm of chromosome 11, confers high and stable resistance to many Chinese rice blast isolates
- The isolation and characterization of Pik, a rice blast resistance gene which emerged after rice domestication
- To study similar, but distinct, plant disease resistance (R) specificities exhibited by allelic genes at the rice blast resistance locus Pik/Pikm, we cloned the Pik gene from rice cultivar Kanto51 and compared its molecular features with those of Pikm and of another Pik gene cloned from cv
- Characterization of the rice blast resistance gene Pik cloned from Kanto51
- Pik is a younger allele at the locus that probably emerged after rice domestication
- Connection
- OsHIPP19, Pik-1, Multiple variants of the fungal effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19, providing a foundation to engineer plant defence, We define the biochemical and structural basis of the interaction between AVR-Pik and OsHIPP19, and compare the interaction to that formed with the HMA domain of Pik-1
- OsHIPP19, Pik-1, Multiple variants of the fungal effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19, providing a foundation to engineer plant defence, Using analytical gel filtration and surface plasmon resonance, we show that multiple AVR-Pik variants, including the stealthy variants AVR-PikC and AVR-PikF which do not interact with any characterised Pik-1 alleles, bind to OsHIPP19 with nanomolar affinity
- OsHIPP19, Pik-1, Multiple variants of the fungal effector AVR-Pik bind the HMA domain of the rice protein OsHIPP19, providing a foundation to engineer plant defence, The crystal structure of OsHIPP19 in complex with AVR-PikF reveals differences at the interface that underpin high-affinity binding of OsHIPP19-HMA to a wider set of AVR-Pik variants than achieved by the integrated HMA domain of Pik-1
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