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Two wheat glutathione peroxidase genes whose products are located in chloroplasts improve salt and H2O2 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...
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Published in: | PloS one 2013-10, Vol.8 (10), p.e73989 |
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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 H2O2 and t-butyl hydroperoxide (t-BHP) using glutathione (GSH) or thioredoxin (Trx) as an electron donor in vitro, showing their peroxidase activity toward H2O2 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, H2O2, 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, H2O2, and ABA treatment in Arabidopsis. Moreover, the expression levels of key regulator genes (SOS1, RbohD and ABI1/ABI2) involved in salt, H2O2 and ABA signaling were altered in the transgenic plants. These findings suggest that W69 and W106 not only act as scavengers of H2O2 in controlling abiotic stress responses, but also play important roles in salt and ABA signaling. |
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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 H2O2 and t-butyl hydroperoxide (t-BHP) using glutathione (GSH) or thioredoxin (Trx) as an electron donor in vitro, showing their peroxidase activity toward H2O2 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, H2O2, 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, H2O2, and ABA treatment in Arabidopsis. Moreover, the expression levels of key regulator genes (SOS1, RbohD and ABI1/ABI2) involved in salt, H2O2 and ABA signaling were altered in the transgenic plants. These findings suggest that W69 and W106 not only act as scavengers of H2O2 in controlling abiotic stress responses, but also play important roles in salt and ABA signaling.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0073989</identifier><identifier>PMID: 24098330</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Abscisic acid ; Agriculture ; Alcohol ; Amino Acid Sequence ; Antioxidants ; Apoptosis ; Arabidopsis ; Arabidopsis - drug effects ; Arabidopsis - genetics ; Arabidopsis - physiology ; Barley ; Biology ; Butyl hydroperoxide ; Chloroplasts ; Chloroplasts - metabolism ; Crop science ; Damage accumulation ; Drought ; Enzymes ; Fluorescence ; Gene expression ; Gene sequencing ; Genes ; Glutathione ; Glutathione peroxidase ; Glutathione Peroxidase - chemistry ; Glutathione Peroxidase - genetics ; Glutathione Peroxidase - metabolism ; Hydrogen peroxide ; Hydrogen Peroxide - pharmacology ; Intracellular Space - metabolism ; Laboratories ; Molecular Sequence Data ; Organic hydroperoxide ; Oxidative stress ; Oxygen ; Pathogens ; Peroxidase ; Plant sciences ; Plants, Genetically Modified ; Polymerase chain reaction ; Protein Transport ; Proteins ; Reactive oxygen species ; Rodents ; Salts ; Seedlings ; Signal transduction ; Signaling ; Sodium Chloride - pharmacology ; Stress, Physiological - drug effects ; Thioredoxin ; Tobacco ; Tolerances ; Transcription factors ; Transgenic plants ; Triticeae ; Triticum - enzymology ; Triticum - genetics ; Triticum aestivum ; Wheat</subject><ispartof>PloS one, 2013-10, Vol.8 (10), p.e73989</ispartof><rights>2013 Zhai et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Zhai et al 2013 Zhai et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-ed5d74b5096e6da1c84b573c57892556859b34ef3f42be012848c9fb231848fd3</citedby><cites>FETCH-LOGICAL-c526t-ed5d74b5096e6da1c84b573c57892556859b34ef3f42be012848c9fb231848fd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1439076431/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1439076431?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24098330$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Bennett, Malcolm</contributor><creatorcontrib>Zhai, Chao-Zeng</creatorcontrib><creatorcontrib>Zhao, Lei</creatorcontrib><creatorcontrib>Yin, Li-Juan</creatorcontrib><creatorcontrib>Chen, Ming</creatorcontrib><creatorcontrib>Wang, Qing-Yu</creatorcontrib><creatorcontrib>Li, Lian-Cheng</creatorcontrib><creatorcontrib>Xu, Zhao-Shi</creatorcontrib><creatorcontrib>Ma, You-Zhi</creatorcontrib><title>Two wheat glutathione peroxidase genes whose products are located in chloroplasts improve salt and H2O2 tolerances in Arabidopsis</title><title>PloS one</title><addtitle>PLoS One</addtitle><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 H2O2 and t-butyl hydroperoxide (t-BHP) using glutathione (GSH) or thioredoxin (Trx) as an electron donor in vitro, showing their peroxidase activity toward H2O2 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, H2O2, 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, H2O2, and ABA treatment in Arabidopsis. Moreover, the expression levels of key regulator genes (SOS1, RbohD and ABI1/ABI2) involved in salt, H2O2 and ABA signaling were altered in the transgenic plants. These findings suggest that W69 and W106 not only act as scavengers of H2O2 in controlling abiotic stress responses, but also play important roles in salt and ABA signaling.</description><subject>Abscisic acid</subject><subject>Agriculture</subject><subject>Alcohol</subject><subject>Amino Acid Sequence</subject><subject>Antioxidants</subject><subject>Apoptosis</subject><subject>Arabidopsis</subject><subject>Arabidopsis - drug effects</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - physiology</subject><subject>Barley</subject><subject>Biology</subject><subject>Butyl hydroperoxide</subject><subject>Chloroplasts</subject><subject>Chloroplasts - metabolism</subject><subject>Crop science</subject><subject>Damage accumulation</subject><subject>Drought</subject><subject>Enzymes</subject><subject>Fluorescence</subject><subject>Gene expression</subject><subject>Gene sequencing</subject><subject>Genes</subject><subject>Glutathione</subject><subject>Glutathione peroxidase</subject><subject>Glutathione Peroxidase - chemistry</subject><subject>Glutathione Peroxidase - genetics</subject><subject>Glutathione Peroxidase - metabolism</subject><subject>Hydrogen peroxide</subject><subject>Hydrogen Peroxide - pharmacology</subject><subject>Intracellular Space - metabolism</subject><subject>Laboratories</subject><subject>Molecular Sequence Data</subject><subject>Organic hydroperoxide</subject><subject>Oxidative stress</subject><subject>Oxygen</subject><subject>Pathogens</subject><subject>Peroxidase</subject><subject>Plant sciences</subject><subject>Plants, Genetically Modified</subject><subject>Polymerase chain reaction</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Reactive oxygen species</subject><subject>Rodents</subject><subject>Salts</subject><subject>Seedlings</subject><subject>Signal transduction</subject><subject>Signaling</subject><subject>Sodium Chloride - pharmacology</subject><subject>Stress, Physiological - drug effects</subject><subject>Thioredoxin</subject><subject>Tobacco</subject><subject>Tolerances</subject><subject>Transcription factors</subject><subject>Transgenic plants</subject><subject>Triticeae</subject><subject>Triticum - 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drug effects</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - physiology</topic><topic>Barley</topic><topic>Biology</topic><topic>Butyl hydroperoxide</topic><topic>Chloroplasts</topic><topic>Chloroplasts - metabolism</topic><topic>Crop science</topic><topic>Damage accumulation</topic><topic>Drought</topic><topic>Enzymes</topic><topic>Fluorescence</topic><topic>Gene expression</topic><topic>Gene sequencing</topic><topic>Genes</topic><topic>Glutathione</topic><topic>Glutathione peroxidase</topic><topic>Glutathione Peroxidase - chemistry</topic><topic>Glutathione Peroxidase - genetics</topic><topic>Glutathione Peroxidase - metabolism</topic><topic>Hydrogen peroxide</topic><topic>Hydrogen Peroxide - pharmacology</topic><topic>Intracellular Space - metabolism</topic><topic>Laboratories</topic><topic>Molecular Sequence Data</topic><topic>Organic hydroperoxide</topic><topic>Oxidative stress</topic><topic>Oxygen</topic><topic>Pathogens</topic><topic>Peroxidase</topic><topic>Plant sciences</topic><topic>Plants, Genetically Modified</topic><topic>Polymerase chain reaction</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Reactive oxygen species</topic><topic>Rodents</topic><topic>Salts</topic><topic>Seedlings</topic><topic>Signal transduction</topic><topic>Signaling</topic><topic>Sodium Chloride - 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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 H2O2 and t-butyl hydroperoxide (t-BHP) using glutathione (GSH) or thioredoxin (Trx) as an electron donor in vitro, showing their peroxidase activity toward H2O2 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, H2O2, 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, H2O2, and ABA treatment in Arabidopsis. Moreover, the expression levels of key regulator genes (SOS1, RbohD and ABI1/ABI2) involved in salt, H2O2 and ABA signaling were altered in the transgenic plants. These findings suggest that W69 and W106 not only act as scavengers of H2O2 in controlling abiotic stress responses, but also play important roles in salt and ABA signaling.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24098330</pmid><doi>10.1371/journal.pone.0073989</doi><oa>free_for_read</oa></addata></record> |
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subjects | Abscisic acid Agriculture Alcohol Amino Acid Sequence Antioxidants Apoptosis Arabidopsis Arabidopsis - drug effects Arabidopsis - genetics Arabidopsis - physiology Barley Biology Butyl hydroperoxide Chloroplasts Chloroplasts - metabolism Crop science Damage accumulation Drought Enzymes Fluorescence Gene expression Gene sequencing Genes Glutathione Glutathione peroxidase Glutathione Peroxidase - chemistry Glutathione Peroxidase - genetics Glutathione Peroxidase - metabolism Hydrogen peroxide Hydrogen Peroxide - pharmacology Intracellular Space - metabolism Laboratories Molecular Sequence Data Organic hydroperoxide Oxidative stress Oxygen Pathogens Peroxidase Plant sciences Plants, Genetically Modified Polymerase chain reaction Protein Transport Proteins Reactive oxygen species Rodents Salts Seedlings Signal transduction Signaling Sodium Chloride - pharmacology Stress, Physiological - drug effects Thioredoxin Tobacco Tolerances Transcription factors Transgenic plants Triticeae Triticum - enzymology Triticum - genetics Triticum aestivum Wheat |
title | Two wheat glutathione peroxidase genes whose products are located in chloroplasts improve salt and H2O2 tolerances in Arabidopsis |
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