HSP90.2 modulates 2Q2‐mediated wheat resistance against powdery mildew

Author:

Yan Yan12,Guo Yue‐Ting23,Chang Chao‐Yan23,Li Xiao‐Ming23,Zhang Mei‐Qi23,Ding Ci‐Hang23,Cui Dangqun1,Sun Congwei1,Ren Yan1,Wang Meng‐Lu3,Xie Chaojie3,Ni Zhongfu3ORCID,Sun Qixin3,Chen Feng1,Gou (缑金营) Jin‐Ying23ORCID

Affiliation:

1. National Key Laboratory of Wheat and Maize Crop Science/CIMMYT‐China Wheat and Maize Improvement Joint Center/College of Agronomy Henan Agricultural University Zhengzhou China

2. School of Life Sciences, Fudan University Shanghai China

3. Key Laboratory of Crop Heterosis and Utilization (MOE), Beijing Key Laboratory of Crop Genetic Improvement China Agricultural University Beijing China

Abstract

AbstractWheat (Triticum aestivum L.) is a critical food crop feeding the world, but pathogens threaten its production. Wheat Heat Shock Protein 90.2 (HSP90.2) is a pathogen‐inducible molecular chaperone folding nascent preproteins. Here, we used wheat HSP90.2 to isolate clients regulated at the posttranslational level. Tetraploid wheat hsp90.2 knockout mutant was susceptible to powdery mildew, while the HSP90.2 overexpression line was resistant, suggesting that HSP90.2 was essential for wheat resistance against powdery mildew. We next isolated 1500 clients of HSP90.2, which contained a wide variety of clients with different biological classifications. We utilized 2Q2, a nucleotide‐binding leucine repeat‐rich protein, as a model to investigate the potential of HSP90.2 interactome in fungal resistance. The transgenic line co‐suppressing 2Q2 was more susceptible to powdery mildew, suggesting 2Q2 as a novel Pm‐resistant gene. The 2Q2 protein resided in chloroplasts, and HSP90.2 played a critical role in the accumulation of 2Q2 in thylakoids. Our data provided over 1500 HSP90.2 clients with a potential regulation at the protein folding process and contributed a nontypical approach to isolate pathogenesis‐related proteins.

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

Plant Science,Physiology

Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3