TuNHL1, an NDR1/HIN1 like gene, is essential for YrU1-mediated stripe rust resistance and enhances powdery mildew resistance in plants.

IF 4.1 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Plant Science Pub Date : 2025-11-01 Epub Date: 2025-08-06 DOI:10.1016/j.plantsci.2025.112701
Jiahao Ji, Yue Xu, Xiaohong Zhang, Yujing Li, Dingzhong Tang, Shenghao Zou
{"title":"TuNHL1, an NDR1/HIN1 like gene, is essential for YrU1-mediated stripe rust resistance and enhances powdery mildew resistance in plants.","authors":"Jiahao Ji, Yue Xu, Xiaohong Zhang, Yujing Li, Dingzhong Tang, Shenghao Zou","doi":"10.1016/j.plantsci.2025.112701","DOIUrl":null,"url":null,"abstract":"<p><p>YrU1 encodes a coiled-coil nucleotide-binding site leucine-rich repeat (CNL) immune receptor with additional ankyrin-repeat and WRKY domains, and confers robust resistance against the stripe rust pathogen Puccinia striiformis f. sp. tritici (Pst). YrU1 was identified through map-based cloning in Triticum urartu accession PI428309, the progenitor species of the A genome of hexaploid wheat. Despite its established role in conferring Pst resistance, the molecular mechanisms and interacting components involved in YrU1-mediated immunity remain largely undefined. In this study, we identified TuNHL1, a plasma membrane-localized NDR1/HIN1-like (NHL) protein, as a key component required for YrU1-mediated stripe rust resistance. TuNHL1 exhibits self-association and is capable of triggering hypersensitive cell death when transiently expressed in Nicotiana benthamiana leaves. Virus-induced gene silencing (VIGS) of TuNHL1 using the barley stripe mosaic virus (BSMV) system in the resistant T. urartu accession PI428309 significantly compromised resistance to the Pst isolate CY33, indicating that TuNHL1 is essential for YrU1-triggered immune responses. Moreover, overexpression of TuNHL1 in both wheat and Arabidopsis thaliana enhanced resistance to powdery mildew following inoculation with their respective pathogens. Taken together, our results revealed important roles of TuNHL1 in YrU1-mediated stripe rust resistance and powdery mildew resistance.</p>","PeriodicalId":20273,"journal":{"name":"Plant Science","volume":" ","pages":"112701"},"PeriodicalIF":4.1000,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Science","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1016/j.plantsci.2025.112701","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/8/6 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

YrU1 encodes a coiled-coil nucleotide-binding site leucine-rich repeat (CNL) immune receptor with additional ankyrin-repeat and WRKY domains, and confers robust resistance against the stripe rust pathogen Puccinia striiformis f. sp. tritici (Pst). YrU1 was identified through map-based cloning in Triticum urartu accession PI428309, the progenitor species of the A genome of hexaploid wheat. Despite its established role in conferring Pst resistance, the molecular mechanisms and interacting components involved in YrU1-mediated immunity remain largely undefined. In this study, we identified TuNHL1, a plasma membrane-localized NDR1/HIN1-like (NHL) protein, as a key component required for YrU1-mediated stripe rust resistance. TuNHL1 exhibits self-association and is capable of triggering hypersensitive cell death when transiently expressed in Nicotiana benthamiana leaves. Virus-induced gene silencing (VIGS) of TuNHL1 using the barley stripe mosaic virus (BSMV) system in the resistant T. urartu accession PI428309 significantly compromised resistance to the Pst isolate CY33, indicating that TuNHL1 is essential for YrU1-triggered immune responses. Moreover, overexpression of TuNHL1 in both wheat and Arabidopsis thaliana enhanced resistance to powdery mildew following inoculation with their respective pathogens. Taken together, our results revealed important roles of TuNHL1 in YrU1-mediated stripe rust resistance and powdery mildew resistance.

TuNHL1是NDR1/HIN1样基因,在yru1介导的植物抗条锈病和增强白粉病抗性中起重要作用。
YrU1编码一个具有附加锚蛋白重复和WRKY结构域的卷曲核苷结合位点富亮氨酸重复序列(CNL)免疫受体,并赋予对条纹锈病病原体小麦锈病(Pst)的强大抗性。通过定位克隆,在乌拉尔图小麦(Triticum urartu)加入PI428309中鉴定出YrU1基因,该基因是小麦六倍体A基因组的祖先种。尽管已确定其在赋予Pst抗性中的作用,但在yru1介导的免疫中所涉及的分子机制和相互作用成分在很大程度上仍不明确。在这项研究中,我们确定了TuNHL1,一个质膜定位的NDR1/ hin1样(NHL)蛋白,是yru1介导的条锈病抗性所需的关键成分。tunh1表现出自我关联,当在烟叶中短暂表达时,能够触发超敏细胞死亡。利用大麦条纹花叶病毒(BSMV)系统对TuNHL1进行病毒诱导的基因沉默(VIGS),显著降低了对Pst分离物CY33的抗性,表明TuNHL1对yru1引发的免疫应答至关重要。此外,在小麦和拟南芥中,TuNHL1的过表达在接种各自的病原体后增强了对白粉病的抗性。综上所述,我们的研究结果揭示了TuNHL1在yru1介导的条锈病抗性和白粉病抗性中发挥重要作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Plant Science
Plant Science 生物-生化与分子生物学
CiteScore
9.10
自引率
1.90%
发文量
322
审稿时长
33 days
期刊介绍: Plant Science will publish in the minimum of time, research manuscripts as well as commissioned reviews and commentaries recommended by its referees in all areas of experimental plant biology with emphasis in the broad areas of genomics, proteomics, biochemistry (including enzymology), physiology, cell biology, development, genetics, functional plant breeding, systems biology and the interaction of plants with the environment. Manuscripts for full consideration should be written concisely and essentially as a final report. The main criterion for publication is that the manuscript must contain original and significant insights that lead to a better understanding of fundamental plant biology. Papers centering on plant cell culture should be of interest to a wide audience and methods employed result in a substantial improvement over existing established techniques and approaches. Methods papers are welcome only when the technique(s) described is novel or provides a major advancement of established protocols.
×
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