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TaRar1 Is Involved in Wheat Defense against Stripe Rust Pathogen Mediated by YrSu

RAR1 is a eukaryotic zinc-binding protein first identified as required for race-specific resistance to powdery mildew in barley. To study the function of TaRAR1 involvement in wheat (Triticum aestivum L.) defense against the infection of stripe rust pathogen Puccinia striiformis f. sp. tritici (Pst)...

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Autores principales: Wang, Xiaojing, Wang, Yaru, Liu, Peng, Ding, Yan, Mu, Xiaoqian, Liu, Xiping, Wang, Xiaojie, Zhao, Mengxin, Huai, Baoyu, Huang, Li, Kang, Zhensheng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5306363/
https://www.ncbi.nlm.nih.gov/pubmed/28261230
http://dx.doi.org/10.3389/fpls.2017.00156
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author Wang, Xiaojing
Wang, Yaru
Liu, Peng
Ding, Yan
Mu, Xiaoqian
Liu, Xiping
Wang, Xiaojie
Zhao, Mengxin
Huai, Baoyu
Huang, Li
Kang, Zhensheng
author_facet Wang, Xiaojing
Wang, Yaru
Liu, Peng
Ding, Yan
Mu, Xiaoqian
Liu, Xiping
Wang, Xiaojie
Zhao, Mengxin
Huai, Baoyu
Huang, Li
Kang, Zhensheng
author_sort Wang, Xiaojing
collection PubMed
description RAR1 is a eukaryotic zinc-binding protein first identified as required for race-specific resistance to powdery mildew in barley. To study the function of TaRAR1 involvement in wheat (Triticum aestivum L.) defense against the infection of stripe rust pathogen Puccinia striiformis f. sp. tritici (Pst), we identified and cloned three wheat homeologous genes highly similar to the barley HvRar1, designated as TaRar1-2A, TaRar1-2B, and TaRar1-2D. The three TaRAR1 proteins all contain two conserved cysteine-and histidine-rich domains (CHORD-I and -II) shared by known RAR1-like proteins. Characterization of TaRar1 expression revealed that the expression was tissue-specific and up-regulated in wheat during stripe rust infection. Moreover, the transcription of TaRar1 was induced by methyl jasmonate, ethylene, and abscisic acid hormones. The same results were observed with drought and wound treatments. After TaRar1 was silenced in wheat cultivar Suwon11 containing the stripe rust resistance gene YrSu, the endogenous salicylic acid (SA) level, the hydrogen peroxide (H(2)O(2)) accumulation and the degree of hypersensitive response (HR) were significantly decreased, and the resistance to the avirulent pathotype of stripe rust was compromised. Meanwhile, the expression of catalase, an enzyme required for H(2)O(2)-scavenging, was up-regulated. Taken together, we concluded that TaRar1 is involved in wheat defense against stripe rust mediated by YrSu, and the defense was through SA to influence reactive oxygen species accumulation and HR.
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spelling pubmed-53063632017-03-03 TaRar1 Is Involved in Wheat Defense against Stripe Rust Pathogen Mediated by YrSu Wang, Xiaojing Wang, Yaru Liu, Peng Ding, Yan Mu, Xiaoqian Liu, Xiping Wang, Xiaojie Zhao, Mengxin Huai, Baoyu Huang, Li Kang, Zhensheng Front Plant Sci Plant Science RAR1 is a eukaryotic zinc-binding protein first identified as required for race-specific resistance to powdery mildew in barley. To study the function of TaRAR1 involvement in wheat (Triticum aestivum L.) defense against the infection of stripe rust pathogen Puccinia striiformis f. sp. tritici (Pst), we identified and cloned three wheat homeologous genes highly similar to the barley HvRar1, designated as TaRar1-2A, TaRar1-2B, and TaRar1-2D. The three TaRAR1 proteins all contain two conserved cysteine-and histidine-rich domains (CHORD-I and -II) shared by known RAR1-like proteins. Characterization of TaRar1 expression revealed that the expression was tissue-specific and up-regulated in wheat during stripe rust infection. Moreover, the transcription of TaRar1 was induced by methyl jasmonate, ethylene, and abscisic acid hormones. The same results were observed with drought and wound treatments. After TaRar1 was silenced in wheat cultivar Suwon11 containing the stripe rust resistance gene YrSu, the endogenous salicylic acid (SA) level, the hydrogen peroxide (H(2)O(2)) accumulation and the degree of hypersensitive response (HR) were significantly decreased, and the resistance to the avirulent pathotype of stripe rust was compromised. Meanwhile, the expression of catalase, an enzyme required for H(2)O(2)-scavenging, was up-regulated. Taken together, we concluded that TaRar1 is involved in wheat defense against stripe rust mediated by YrSu, and the defense was through SA to influence reactive oxygen species accumulation and HR. Frontiers Media S.A. 2017-02-14 /pmc/articles/PMC5306363/ /pubmed/28261230 http://dx.doi.org/10.3389/fpls.2017.00156 Text en Copyright © 2017 Wang, Wang, Liu, Ding, Mu, Liu, Wang, Zhao, Huai, Huang and Kang. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Wang, Xiaojing
Wang, Yaru
Liu, Peng
Ding, Yan
Mu, Xiaoqian
Liu, Xiping
Wang, Xiaojie
Zhao, Mengxin
Huai, Baoyu
Huang, Li
Kang, Zhensheng
TaRar1 Is Involved in Wheat Defense against Stripe Rust Pathogen Mediated by YrSu
title TaRar1 Is Involved in Wheat Defense against Stripe Rust Pathogen Mediated by YrSu
title_full TaRar1 Is Involved in Wheat Defense against Stripe Rust Pathogen Mediated by YrSu
title_fullStr TaRar1 Is Involved in Wheat Defense against Stripe Rust Pathogen Mediated by YrSu
title_full_unstemmed TaRar1 Is Involved in Wheat Defense against Stripe Rust Pathogen Mediated by YrSu
title_short TaRar1 Is Involved in Wheat Defense against Stripe Rust Pathogen Mediated by YrSu
title_sort tarar1 is involved in wheat defense against stripe rust pathogen mediated by yrsu
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5306363/
https://www.ncbi.nlm.nih.gov/pubmed/28261230
http://dx.doi.org/10.3389/fpls.2017.00156
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