A wheat tandem kinase activates an NLR to trigger immunity

• 成果类型: Article
• 署名作者: Chen, Renjie; Chen, Jian; Powell, Oliver R.; Outram, Megan A.; Arndell, Taj; Gajendiran, Karthick; Wang, Yan L.; Lubega, Jibril; Xu, Yang; Ayliffe, Michael A.; Blundell, Cheryl; Figueroa, Melania; Sperschneider, Jana; Vanhercke, Thomas; Kanyuka, Kostya; Tang, Dingzhong; Zhong, Guitao; Gardener, Catherine; Yu, Guotai; Gourdoupis, Spyridon; Jaremko, Lukasz; Matny, Oadi; Steffenson, Brian J.; Boshoff, Willem H. P.; Meyer, Wilku B.; Arold, Stefan T.; Dodds, Peter N.; Wulff, Brande B. H.
• 署名单位: King Abdullah University of Science & Technology; Commonwealth Scientific & Industrial Research Organisation (CSIRO); CSIRO Agriculture & Food; Fujian Agriculture & Forestry University; King Abdullah University of Science & Technology; University of Minnesota System; University of Minnesota Twin Cities; University of the Free State
• 刊物名称: SCIENCE
• ISSN/ISSBN: 0036-13973
• DOI: 10.1126/science.adp5034
• 发表日期: 2025-03-28
• 页码: 1402-1408
• 关键词: resistance

摘要

The role of nucleotide-binding leucine-rich repeat (NLR) receptors in plant immunity is well studied, but the function of a class of tandem kinases (TKs) that confer disease resistance in wheat and barley remains unclear. In this study, we show that the SR62 locus is a digenic module encoding the Sr62TK TK and an NLR (Sr62NLR), and we identify the corresponding AvrSr62 effector. AvrSr62 binds to the N-terminal kinase 1 of Sr62TK, triggering displacement of kinase 2, which activates Sr62NLR. Modeling and mutation analysis indicated that this is mediated by overlapping binding sites (i) on kinase 1 for binding AvrSr62 and kinase 2 and (ii) on kinase 2 for binding kinase 1 and Sr62NLR. Understanding this two-component resistance complex may help engineering and breeding plants for durable resistance.