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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Shrnutí: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.
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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
ISSN:1664-462X
1664-462X
DOI:10.3389/fpls.2020.00231