Expression of Heterologous OsDHAR Gene Improves Glutathione (GSH)-Dependent Antioxidant System and Maintenance of Cellular Redox Status in Synechococcus elongatus PCC 7942

An excess of reactive oxygen species (ROS) can cause severe oxidative damage to cellular components in photosynthetic cells. Antioxidant systems, such as the glutathione (GSH) pools, regulate redox status in cells to guard against such damage. Dehydroascorbate reductase (DHAR, EC 1.8.5.1) catalyzes...

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Vydáno v:	Frontiers in plant science Ročník 11; s. 231
Hlavní autoři:	Kim, Young-Saeng, Park, Seong-Im, Kim, Jin-Ju, Boyd, Joseph S., Beld, Joris, Taton, Arnaud, Lee, Kyoung-In, Kim, Il-Sup, Golden, James W., Yoon, Ho-Sung
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Switzerland Frontiers Media SA 03.03.2020 Frontiers Media S.A
Témata:	Abiotic stress antioxidant-related enzymes Antioxidants Ascorbic acid Binding sites Cloning Cyanobacteria cyanobacterium Damage dehydroascorbate reductase Elongation Enzymes Glutathione Homeostasis Hydrogen peroxide Oxidative stress Physiology Plant Science Plasmids Proteins Reactive oxygen species Reductases Synechococcus elongatus Tobacco antioxidant-related enzymes cyanobacterium antioxidants dehydroascorbate reductase oxidative stress
ISSN:	1664-462X, 1664-462X
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Abstract	An excess of reactive oxygen species (ROS) can cause severe oxidative damage to cellular components in photosynthetic cells. Antioxidant systems, such as the glutathione (GSH) pools, regulate redox status in cells to guard against such damage. Dehydroascorbate reductase (DHAR, EC 1.8.5.1) catalyzes the glutathione-dependent reduction of oxidized ascorbate (dehydroascorbate) and contains a redox active site and glutathione binding-site. The gene is important in biological and abiotic stress responses involving reduction of the oxidative damage caused by ROS. In this study, transgenic PCC 7942 (TA) was constructed by cloning the L. ( ) gene controlled by an isopropyl β-D-1-thiogalactopyranoside (IPTG)-inducible promoter ( ) into the cyanobacterium to study the functional activities of under oxidative stress caused by hydrogen peroxide exposure. expression increased the growth of PCC 7942 under oxidative stress by reducing the levels of hydroperoxides and malondialdehyde (MDA) and mitigating the loss of chlorophyll. DHAR and glutathione -transferase activity were higher than in the wild-type PCC 7942 (WT). Additionally, overexpression of in PCC 7942 greatly increased the glutathione (GSH)/glutathione disulfide (GSSG) ratio in the presence or absence of hydrogen peroxide. These results strongly suggest that attenuates deleterious oxidative effects via the glutathione (GSH)-dependent antioxidant system in cyanobacterial cells. The expression of heterologous in PCC 7942 protected cells from oxidative damage through a GSH-dependent antioxidant system via GSH-dependent reactions at the redox active site and GSH binding site residues during oxidative stress.
AbstractList	An excess of reactive oxygen species (ROS) can cause severe oxidative damage to cellular components in photosynthetic cells. Antioxidant systems, such as the glutathione (GSH) pools, regulate redox status in cells to guard against such damage. Dehydroascorbate reductase (DHAR, EC 1.8.5.1) catalyzes the glutathione-dependent reduction of oxidized ascorbate (dehydroascorbate) and contains a redox active site and glutathione binding-site. The DHAR gene is important in biological and abiotic stress responses involving reduction of the oxidative damage caused by ROS. In this study, transgenic Synechococcus elongatus PCC 7942 (TA) was constructed by cloning the Oryza sativa L. japonica DHAR (OsDHAR) gene controlled by an isopropyl β-D-1-thiogalactopyranoside (IPTG)-inducible promoter (Ptrc) into the cyanobacterium to study the functional activities of OsDHAR under oxidative stress caused by hydrogen peroxide exposure. OsDHAR expression increased the growth of S. elongatus PCC 7942 under oxidative stress by reducing the levels of hydroperoxides and malondialdehyde (MDA) and mitigating the loss of chlorophyll. DHAR and glutathione S-transferase activity were higher than in the wild-type S. elongatus PCC 7942 (WT). Additionally, overexpression of OsDHAR in S. elongatus PCC 7942 greatly increased the glutathione (GSH)/glutathione disulfide (GSSG) ratio in the presence or absence of hydrogen peroxide. These results strongly suggest that DHAR attenuates deleterious oxidative effects via the glutathione (GSH)-dependent antioxidant system in cyanobacterial cells. The expression of heterologous OsDHAR in S. elongatus PCC 7942 protected cells from oxidative damage through a GSH-dependent antioxidant system via GSH-dependent reactions at the redox active site and GSH binding site residues during oxidative stress. An excess of reactive oxygen species (ROS) can cause severe oxidative damage to cellular components in photosynthetic cells. Antioxidant systems, such as the glutathione (GSH) pools, regulate redox status in cells to guard against such damage. Dehydroascorbate reductase (DHAR, EC 1.8.5.1) catalyzes the glutathione-dependent reduction of oxidized ascorbate (dehydroascorbate) and contains a redox active site and glutathione binding-site. The gene is important in biological and abiotic stress responses involving reduction of the oxidative damage caused by ROS. In this study, transgenic PCC 7942 (TA) was constructed by cloning the L. ( ) gene controlled by an isopropyl β-D-1-thiogalactopyranoside (IPTG)-inducible promoter ( ) into the cyanobacterium to study the functional activities of under oxidative stress caused by hydrogen peroxide exposure. expression increased the growth of PCC 7942 under oxidative stress by reducing the levels of hydroperoxides and malondialdehyde (MDA) and mitigating the loss of chlorophyll. DHAR and glutathione -transferase activity were higher than in the wild-type PCC 7942 (WT). Additionally, overexpression of in PCC 7942 greatly increased the glutathione (GSH)/glutathione disulfide (GSSG) ratio in the presence or absence of hydrogen peroxide. These results strongly suggest that attenuates deleterious oxidative effects via the glutathione (GSH)-dependent antioxidant system in cyanobacterial cells. The expression of heterologous in PCC 7942 protected cells from oxidative damage through a GSH-dependent antioxidant system via GSH-dependent reactions at the redox active site and GSH binding site residues during oxidative stress. An excess of reactive oxygen species (ROS) can cause severe oxidative damage to cellular components in photosynthetic cells. Antioxidant systems, such as the glutathione (GSH) pools, regulate redox status in cells to guard against such damage. Dehydroascorbate reductase (DHAR, EC 1.8.5.1) catalyzes the glutathione-dependent reduction of oxidized ascorbate (dehydroascorbate) and contains a redox active site and glutathione binding-site. The DHAR gene is important in biological and abiotic stress responses involving reduction of the oxidative damage caused by ROS. In this study, transgenic Synechococcus elongatus PCC 7942 (TA) was constructed by cloning the Oryza sativa L. japonica DHAR (OsDHAR) gene controlled by an isopropyl β-D-1-thiogalactopyranoside (IPTG)-inducible promoter (Ptrc) into the cyanobacterium to study the functional activities of OsDHAR under oxidative stress caused by hydrogen peroxide exposure. OsDHAR expression increased the growth of S. elongatus PCC 7942 under oxidative stress by reducing the levels of hydroperoxides and malondialdehyde (MDA) and mitigating the loss of chlorophyll. DHAR and glutathione S-transferase activity were higher than in the wild-type S. elongatus PCC 7942 (WT). Additionally, overexpression of OsDHAR in S. elongatus PCC 7942 greatly increased the glutathione (GSH)/glutathione disulfide (GSSG) ratio in the presence or absence of hydrogen peroxide. These results strongly suggest that DHAR attenuates deleterious oxidative effects via the glutathione (GSH)-dependent antioxidant system in cyanobacterial cells. The expression of heterologous OsDHAR in S. elongatus PCC 7942 protected cells from oxidative damage through a GSH-dependent antioxidant system via GSH-dependent reactions at the redox active site and GSH binding site residues during oxidative stress.An excess of reactive oxygen species (ROS) can cause severe oxidative damage to cellular components in photosynthetic cells. Antioxidant systems, such as the glutathione (GSH) pools, regulate redox status in cells to guard against such damage. Dehydroascorbate reductase (DHAR, EC 1.8.5.1) catalyzes the glutathione-dependent reduction of oxidized ascorbate (dehydroascorbate) and contains a redox active site and glutathione binding-site. The DHAR gene is important in biological and abiotic stress responses involving reduction of the oxidative damage caused by ROS. In this study, transgenic Synechococcus elongatus PCC 7942 (TA) was constructed by cloning the Oryza sativa L. japonica DHAR (OsDHAR) gene controlled by an isopropyl β-D-1-thiogalactopyranoside (IPTG)-inducible promoter (Ptrc) into the cyanobacterium to study the functional activities of OsDHAR under oxidative stress caused by hydrogen peroxide exposure. OsDHAR expression increased the growth of S. elongatus PCC 7942 under oxidative stress by reducing the levels of hydroperoxides and malondialdehyde (MDA) and mitigating the loss of chlorophyll. DHAR and glutathione S-transferase activity were higher than in the wild-type S. elongatus PCC 7942 (WT). Additionally, overexpression of OsDHAR in S. elongatus PCC 7942 greatly increased the glutathione (GSH)/glutathione disulfide (GSSG) ratio in the presence or absence of hydrogen peroxide. These results strongly suggest that DHAR attenuates deleterious oxidative effects via the glutathione (GSH)-dependent antioxidant system in cyanobacterial cells. The expression of heterologous OsDHAR in S. elongatus PCC 7942 protected cells from oxidative damage through a GSH-dependent antioxidant system via GSH-dependent reactions at the redox active site and GSH binding site residues during oxidative stress.
Author	Beld, Joris Kim, Il-Sup Kim, Jin-Ju Taton, Arnaud Boyd, Joseph S. Golden, James W. Kim, Young-Saeng Yoon, Ho-Sung Lee, Kyoung-In Park, Seong-Im
AuthorAffiliation	3 Department of Biology, Kyungpook National University , Daegu , South Korea 2 School of Life Sciences, BK21 Plus KNU Creative BioResearch Group, Kyungpook National University , Daegu , South Korea 6 Biotechnology Industrialization Center, Dongshin University , Naju , South Korea 5 Department of Microbiology and Immunology, College of Medicine, Drexel University , Philadelphia, PA , United States 7 Advanced Bio Resource Research Center, Kyungpook National University , Daegu , South Korea 4 Division of Biological Sciences, University of California , San Diego, La Jolla, CA , United States 1 Research Institute for Dok-do and Ulleung-do, Kyungpook National University , Daegu , South Korea
AuthorAffiliation_xml	– name: 2 School of Life Sciences, BK21 Plus KNU Creative BioResearch Group, Kyungpook National University , Daegu , South Korea – name: 3 Department of Biology, Kyungpook National University , Daegu , South Korea – name: 5 Department of Microbiology and Immunology, College of Medicine, Drexel University , Philadelphia, PA , United States – name: 7 Advanced Bio Resource Research Center, Kyungpook National University , Daegu , South Korea – name: 1 Research Institute for Dok-do and Ulleung-do, Kyungpook National University , Daegu , South Korea – name: 4 Division of Biological Sciences, University of California , San Diego, La Jolla, CA , United States – name: 6 Biotechnology Industrialization Center, Dongshin University , Naju , South Korea
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Copyright	Copyright © 2020 Kim, Park, Kim, Boyd, Beld, Taton, Lee, Kim, Golden and Yoon. 2020. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. Copyright © 2020 Kim, Park, Kim, Boyd, Beld, Taton, Lee, Kim, Golden and Yoon. 2020 Kim, Park, Kim, Boyd, Beld, Taton, Lee, Kim, Golden and Yoon
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Keywords	antioxidant-related enzymes cyanobacterium antioxidants dehydroascorbate reductase oxidative stress
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Edited by: Dimitris Petroutsos, UMR 5168 Laboratoire de Physiologie Cellulaire Vegetale (LPCV), France Reviewed by: Corinne Cassier-Chauvat, UMR 9198 Institut de Biologie Intégrative de la Cellule (I2BC), France; Sang-Soo Kwak, Korea Research Institute of Bioscience and Biotechnology (KRIBB), South Korea; Muriel Gugger, Institut Pasteur, France This article was submitted to Plant Biotechnology, a section of the journal Frontiers in Plant Science
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Snippet	An excess of reactive oxygen species (ROS) can cause severe oxidative damage to cellular components in photosynthetic cells. Antioxidant systems, such as the...
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SubjectTerms	Abiotic stress antioxidant-related enzymes Antioxidants Ascorbic acid Binding sites Cloning Cyanobacteria cyanobacterium Damage dehydroascorbate reductase Elongation Enzymes Glutathione Homeostasis Hydrogen peroxide Oxidative stress Physiology Plant Science Plasmids Proteins Reactive oxygen species Reductases Synechococcus elongatus Tobacco
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Title	Expression of Heterologous OsDHAR Gene Improves Glutathione (GSH)-Dependent Antioxidant System and Maintenance of Cellular Redox Status in Synechococcus elongatus PCC 7942
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