小麦串联激酶激活NLR触发免疫

IF 45.8 1区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES
Science Pub Date : 2025-03-27 DOI:10.1126/science.adp5034
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,&nbsp;Jian Chen,&nbsp;Oliver R. Powell,&nbsp;Megan A. Outram,&nbsp;Taj Arndell,&nbsp;Karthick Gajendiran,&nbsp;Yan L. Wang,&nbsp;Jibril Lubega,&nbsp;Yang Xu,&nbsp;Michael A. Ayliffe,&nbsp;Cheryl Blundell,&nbsp;Melania Figueroa,&nbsp;Jana Sperschneider,&nbsp;Thomas Vanhercke,&nbsp;Kostya Kanyuka,&nbsp;Dingzhong Tang,&nbsp;Guitao Zhong,&nbsp;Catherine Gardener,&nbsp;Guotai Yu,&nbsp;Spyridon Gourdoupis,&nbsp;Łukasz Jaremko,&nbsp;Oadi Matny,&nbsp;Brian J. Steffenson,&nbsp;Willem H. P. Boshoff,&nbsp;Wilku B. Meyer,&nbsp;Stefan T. Arold,&nbsp;Peter N. Dodds,&nbsp;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,&nbsp;Jian Chen,&nbsp;Oliver R. Powell,&nbsp;Megan A. Outram,&nbsp;Taj Arndell,&nbsp;Karthick Gajendiran,&nbsp;Yan L. Wang,&nbsp;Jibril Lubega,&nbsp;Yang Xu,&nbsp;Michael A. Ayliffe,&nbsp;Cheryl Blundell,&nbsp;Melania Figueroa,&nbsp;Jana Sperschneider,&nbsp;Thomas Vanhercke,&nbsp;Kostya Kanyuka,&nbsp;Dingzhong Tang,&nbsp;Guitao Zhong,&nbsp;Catherine Gardener,&nbsp;Guotai Yu,&nbsp;Spyridon Gourdoupis,&nbsp;Łukasz Jaremko,&nbsp;Oadi Matny,&nbsp;Brian J. Steffenson,&nbsp;Willem H. P. Boshoff,&nbsp;Wilku B. Meyer,&nbsp;Stefan T. Arold,&nbsp;Peter N. Dodds,&nbsp;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}
引用次数: 0

摘要

核苷酸结合的富亮氨酸重复(NLR)受体在植物免疫中的作用已被深入研究,但一类串联激酶(TK)在小麦和大麦中赋予抗病性的功能仍不清楚。在本研究中,我们发现 SR62 基因座是一个编码 Sr62 TK TK 和一个 NLR(Sr62 NLR)的二基因模块,并确定了相应的 AvrSr62 效应子。AvrSr62 与 Sr62 TK 的 N 端激酶 1 结合,引发激酶 2 位移,从而激活 Sr62 NLR。建模和突变分析表明,这是通过重叠的结合位点介导的:(i) 结合 AvrSr62 和激酶 2 的激酶 1;(ii) 结合激酶 1 和 Sr62 NLR 的激酶 2。了解这种双组分抗性复合体可能有助于工程设计和培育具有持久抗性的植物。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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.
求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Science
Science 综合性期刊-综合性期刊
CiteScore
61.10
自引率
0.90%
发文量
0
审稿时长
2.1 months
期刊介绍: Science is a leading outlet for scientific news, commentary, and cutting-edge research. Through its print and online incarnations, Science reaches an estimated worldwide readership of more than one million. Science’s authorship is global too, and its articles consistently rank among the world's most cited research. Science serves as a forum for discussion of important issues related to the advancement of science by publishing material on which a consensus has been reached as well as including the presentation of minority or conflicting points of view. Accordingly, all articles published in Science—including editorials, news and comment, and book reviews—are signed and reflect the individual views of the authors and not official points of view adopted by AAAS or the institutions with which the authors are affiliated. Science seeks to publish those papers that are most influential in their fields or across fields and that will significantly advance scientific understanding. Selected papers should present novel and broadly important data, syntheses, or concepts. They should merit recognition by the wider scientific community and general public provided by publication in Science, beyond that provided by specialty journals. Science welcomes submissions from all fields of science and from any source. The editors are committed to the prompt evaluation and publication of submitted papers while upholding high standards that support reproducibility of published research. Science is published weekly; selected papers are published online ahead of print.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信