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Two Wheat Glutathione Peroxidase Genes Whose Products Are Located in Chloroplasts Improve Salt and H(2)O(2) Tolerances in Arabidopsis
Oxidative stress caused by accumulation of reactive oxygen species (ROS) is capable of damaging effects on numerous cellular components. Glutathione peroxidases (GPXs, EC 1.11.1.9) are key enzymes of the antioxidant network in plants. In this study, W69 and W106, two putative GPX genes, were obtaine...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3788784/ https://www.ncbi.nlm.nih.gov/pubmed/24098330 http://dx.doi.org/10.1371/journal.pone.0073989 |
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author | Zhai, Chao-Zeng Zhao, Lei Yin, Li-Juan Chen, Ming Wang, Qing-Yu Li, Lian-Cheng Xu, Zhao-Shi Ma, You-Zhi |
author_facet | Zhai, Chao-Zeng Zhao, Lei Yin, Li-Juan Chen, Ming Wang, Qing-Yu Li, Lian-Cheng Xu, Zhao-Shi Ma, You-Zhi |
author_sort | Zhai, Chao-Zeng |
collection | PubMed |
description | Oxidative stress caused by accumulation of reactive oxygen species (ROS) is capable of damaging effects on numerous cellular components. Glutathione peroxidases (GPXs, EC 1.11.1.9) are key enzymes of the antioxidant network in plants. In this study, W69 and W106, two putative GPX genes, were obtained by de novo transcriptome sequencing of salt-treated wheat (Triticum aestivum) seedlings. The purified His-tag fusion proteins of W69 and W106 reduced H(2)O(2) and t-butyl hydroperoxide (t-BHP) using glutathione (GSH) or thioredoxin (Trx) as an electron donor in vitro, showing their peroxidase activity toward H(2)O(2) and toxic organic hydroperoxide. GFP fluorescence assays revealed that W69 and W106 are localized in chloroplasts. Quantitative real-time PCR (Q-RT-PCR) analysis showed that two GPXs were differentially responsive to salt, drought, H(2)O(2,) or ABA. Isolation of the W69 and W106 promoters revealed some cis-acting elements responding to abiotic stresses. Overexpression of W69 and W106 conferred strong tolerance to salt, H(2)O(2), and ABA treatment in Arabidopsis. Moreover, the expression levels of key regulator genes (SOS1, RbohD and ABI1/ABI2) involved in salt, H(2)O(2) and ABA signaling were altered in the transgenic plants. These findings suggest that W69 and W106 not only act as scavengers of H(2)O(2) in controlling abiotic stress responses, but also play important roles in salt and ABA signaling. |
format | Online Article Text |
id | pubmed-3788784 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-37887842013-10-04 Two Wheat Glutathione Peroxidase Genes Whose Products Are Located in Chloroplasts Improve Salt and H(2)O(2) Tolerances in Arabidopsis Zhai, Chao-Zeng Zhao, Lei Yin, Li-Juan Chen, Ming Wang, Qing-Yu Li, Lian-Cheng Xu, Zhao-Shi Ma, You-Zhi PLoS One Research Article Oxidative stress caused by accumulation of reactive oxygen species (ROS) is capable of damaging effects on numerous cellular components. Glutathione peroxidases (GPXs, EC 1.11.1.9) are key enzymes of the antioxidant network in plants. In this study, W69 and W106, two putative GPX genes, were obtained by de novo transcriptome sequencing of salt-treated wheat (Triticum aestivum) seedlings. The purified His-tag fusion proteins of W69 and W106 reduced H(2)O(2) and t-butyl hydroperoxide (t-BHP) using glutathione (GSH) or thioredoxin (Trx) as an electron donor in vitro, showing their peroxidase activity toward H(2)O(2) and toxic organic hydroperoxide. GFP fluorescence assays revealed that W69 and W106 are localized in chloroplasts. Quantitative real-time PCR (Q-RT-PCR) analysis showed that two GPXs were differentially responsive to salt, drought, H(2)O(2,) or ABA. Isolation of the W69 and W106 promoters revealed some cis-acting elements responding to abiotic stresses. Overexpression of W69 and W106 conferred strong tolerance to salt, H(2)O(2), and ABA treatment in Arabidopsis. Moreover, the expression levels of key regulator genes (SOS1, RbohD and ABI1/ABI2) involved in salt, H(2)O(2) and ABA signaling were altered in the transgenic plants. These findings suggest that W69 and W106 not only act as scavengers of H(2)O(2) in controlling abiotic stress responses, but also play important roles in salt and ABA signaling. Public Library of Science 2013-10-02 /pmc/articles/PMC3788784/ /pubmed/24098330 http://dx.doi.org/10.1371/journal.pone.0073989 Text en © 2013 Zhai et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Zhai, Chao-Zeng Zhao, Lei Yin, Li-Juan Chen, Ming Wang, Qing-Yu Li, Lian-Cheng Xu, Zhao-Shi Ma, You-Zhi Two Wheat Glutathione Peroxidase Genes Whose Products Are Located in Chloroplasts Improve Salt and H(2)O(2) Tolerances in Arabidopsis |
title | Two Wheat Glutathione Peroxidase Genes Whose Products Are Located in Chloroplasts Improve Salt and H(2)O(2) Tolerances in Arabidopsis
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title_full | Two Wheat Glutathione Peroxidase Genes Whose Products Are Located in Chloroplasts Improve Salt and H(2)O(2) Tolerances in Arabidopsis
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title_fullStr | Two Wheat Glutathione Peroxidase Genes Whose Products Are Located in Chloroplasts Improve Salt and H(2)O(2) Tolerances in Arabidopsis
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title_full_unstemmed | Two Wheat Glutathione Peroxidase Genes Whose Products Are Located in Chloroplasts Improve Salt and H(2)O(2) Tolerances in Arabidopsis
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title_short | Two Wheat Glutathione Peroxidase Genes Whose Products Are Located in Chloroplasts Improve Salt and H(2)O(2) Tolerances in Arabidopsis
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title_sort | two wheat glutathione peroxidase genes whose products are located in chloroplasts improve salt and h(2)o(2) tolerances in arabidopsis |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3788784/ https://www.ncbi.nlm.nih.gov/pubmed/24098330 http://dx.doi.org/10.1371/journal.pone.0073989 |
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