Concurrent Session
Oliver Powell
King Abdullah University of Science and Technology (KAUST)
Thuwal, SAUDI ARABIA
Renjie Chen
Dr.
King Abdullah University of Science and Technology (KAUST)
Thuwal, Makkah, Saudi Arabia
Jian Chen
CSIRO
Canberra, Australian Capital Territory, Australia
Megan Outram
CSIRO
Canberra, Australian Capital Territory, Australia
Peter Dodds, PhD
CSIRO Agriculture and Food
Canberra, ACT, AUSTRALIA
Brande Wulff
Prof. Dr.
King Abdullah University of Science and Technology (KAUST)
Thuwal, Makkah, Saudi Arabia
The structure, function and mechanism of nucleotide-binding and leucine-rich repeat (NLR) receptors in plant immunity is well studied. In comparison the mechanism of kinase fusion proteins (KFPs) an emerging class of immune receptors, in wheat and barley, is poorly understood. In this study, we investigated the mechanism of Sr62-mediated resistance. We cloned an NLR (Sr62NLR) required for the function of Sr62TK and demonstrate that the two genes form a digenic sensor-helper pair at the SR62 locus. Additionally, we cloned the corresponding fungal effector (AvrSr62) that is recognised by Sr62TK. AlphaFold modelling of the Sr62TKrevealed that an unusual extended ß-finger motif in the kinase 1 domain of Sr62TK is crucial for functional dimerization. The motif also acts as the binding surface of the effector. Recognition of AvrSr62 by the kinase 1 domain of Sr62TK triggers displacement of the kinase 2 domain of Sr62TK which activates Sr62NLR and leads to an immune response. The extended ß-finger motif was also identified as a “hotspot” of natural amino acid variation in Sr62TK across Aegilops and Triticeae. Further structural predictions of all previously cloned KFPs highlight that the extended ß-finger motif is near-ubiquitous in KFPs. These findings provide insights into the mechanism of KFP-mediated immunity that will facilitate the engineering and breeding of plants with durable resistance.