Renjie Chen, Jian Chen, Oliver R. Powell, Megan A. Outram, Taj Arndell, Karthick Gajendiran, Yan L. Wang, Jibril Lubega, Yang Xu, Michael A. Ayliffe, Cheryl Blundell, Melania Figueroa, Jana Sperschneider, Thomas Vanhercke, Kostya Kanyuka, Dingzhong Tang, Guitao Zhong, Catherine Gardener, Guotai Yu, Spyridon Gourdoupis, Łukasz Jaremko, Oadi Matny, Brian J. Steffenson, Willem H. P. Boshoff, Wilku B. Meyer, Stefan T. Arold, Peter N. Dodds, Brande B. H. Wulff
{"title":"小麦串联激酶激活NLR触发免疫","authors":"Renjie Chen, Jian Chen, Oliver R. Powell, Megan A. Outram, Taj Arndell, Karthick Gajendiran, Yan L. Wang, Jibril Lubega, Yang Xu, Michael A. Ayliffe, Cheryl Blundell, Melania Figueroa, Jana Sperschneider, Thomas Vanhercke, Kostya Kanyuka, Dingzhong Tang, Guitao Zhong, Catherine Gardener, Guotai Yu, Spyridon Gourdoupis, Łukasz Jaremko, Oadi Matny, Brian J. Steffenson, Willem H. P. Boshoff, Wilku B. Meyer, Stefan T. Arold, Peter N. Dodds, Brande B. H. Wulff","doi":"10.1126/science.adp5034","DOIUrl":null,"url":null,"abstract":"<div >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 <i>SR62</i> locus is a digenic module encoding the Sr62<sup>TK</sup> TK and an NLR (Sr62<sup>NLR</sup>), and we identify the corresponding AvrSr62 effector. AvrSr62 binds to the N-terminal kinase 1 of Sr62<sup>TK</sup>, triggering displacement of kinase 2, which activates Sr62<sup>NLR</sup>. 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 Sr62<sup>NLR</sup>. Understanding this two-component resistance complex may help engineering and breeding plants for durable resistance.</div>","PeriodicalId":21678,"journal":{"name":"Science","volume":"387 6741","pages":""},"PeriodicalIF":45.8000,"publicationDate":"2025-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A wheat tandem kinase activates an NLR to trigger immunity\",\"authors\":\"Renjie Chen, Jian Chen, Oliver R. Powell, Megan A. Outram, Taj Arndell, Karthick Gajendiran, Yan L. Wang, Jibril Lubega, Yang Xu, Michael A. Ayliffe, Cheryl Blundell, Melania Figueroa, Jana Sperschneider, Thomas Vanhercke, Kostya Kanyuka, Dingzhong Tang, Guitao Zhong, Catherine Gardener, Guotai Yu, Spyridon Gourdoupis, Łukasz Jaremko, Oadi Matny, Brian J. Steffenson, Willem H. P. Boshoff, Wilku B. Meyer, Stefan T. Arold, Peter N. Dodds, Brande B. H. Wulff\",\"doi\":\"10.1126/science.adp5034\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div >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 <i>SR62</i> locus is a digenic module encoding the Sr62<sup>TK</sup> TK and an NLR (Sr62<sup>NLR</sup>), and we identify the corresponding AvrSr62 effector. AvrSr62 binds to the N-terminal kinase 1 of Sr62<sup>TK</sup>, triggering displacement of kinase 2, which activates Sr62<sup>NLR</sup>. 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 Sr62<sup>NLR</sup>. Understanding this two-component resistance complex may help engineering and breeding plants for durable resistance.</div>\",\"PeriodicalId\":21678,\"journal\":{\"name\":\"Science\",\"volume\":\"387 6741\",\"pages\":\"\"},\"PeriodicalIF\":45.8000,\"publicationDate\":\"2025-03-27\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Science\",\"FirstCategoryId\":\"103\",\"ListUrlMain\":\"https://www.science.org/doi/10.1126/science.adp5034\",\"RegionNum\":1,\"RegionCategory\":\"综合性期刊\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"MULTIDISCIPLINARY SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Science","FirstCategoryId":"103","ListUrlMain":"https://www.science.org/doi/10.1126/science.adp5034","RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
A wheat tandem kinase activates an NLR to trigger immunity
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.
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