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glutathione reductase/arabidopsis
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Molecular cloning and characterization of the glutathione reductase gene from Stipa purpurea.
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Reactive oxygen species (ROS) are a key factor in abiotic stresses; excess ROS is harmful to plants. Glutathione reductase (GR) plays an important role in scavenging ROS in plants. Here, a GR gene, named SpGR, was cloned from Stipa purpurea and characterized. The full-length open reading frame was
Molecular cloning and characterization of the gene encoding glutathione reductase in Brassica campestris.
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We have isolated the Brassica campestris cDNA encoding glutathione reductase of 502 amino acid residues with molecular mass of 54.5 kDa. The deduced amino acid sequences were 92.2%, and 79.5% identical to those of Arabidopsis thaliana, and pea, respectively. As expected, it exhibited a high degree
Cloning, sequencing, and regulation of the glutathione reductase gene from the cyanobacterium Anabaena PCC 7120.
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Glutathione reductase (GR) was purified from the cyanobacterium Anabaena PCC 7120. A 3-kilobase genomic DNA fragment containing the coding sequence for the GR gene (gor) was identified and cloned by polymerase chain reaction based on sequences of selected peptides isolated from proteolyzed GR. The
Glutathione Reductase Gene Expression Depends on Chloroplast Signals in Arabidopsis thaliana.
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Glutathione reductase (EC 1.6.4.2) is one of the main antioxidant enzymes of the plant cell. In Arabidopsis thaliana, glutathione reductase is encoded by two genes: the gr1 gene encodes the cytosolic-peroxisomal form, and the gr2 gene encodes the chloroplast-mitochondrial form. Little is known about
Chloroplasts Require Glutathione Reductase to Balance Reactive Oxygen Species and Maintain Efficient Photosynthesis.
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Thiol-based redox-regulation is vital to coordinate chloroplast functions depending on illumination and is well investigated for thioredoxin-dependent processes. In parallel, glutathione reductase (GR) maintains a highly reduced glutathione pool, enabling glutathione-mediated redox buffering. Yet,
Arabidopsis glutathione reductase 2 is indispensable in plastids, while mitochondrial glutathione is safeguarded by additional reduction and transport systems.
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A highly negative glutathione redox potential (EGSH ) is maintained in the cytosol, plastids and mitochondria of plant cells to support fundamental processes, including antioxidant defence, redox regulation and iron-sulfur cluster biogenesis. Out of two glutathione reductase (GR) proteins
Analysis of cytosolic isocitrate dehydrogenase and glutathione reductase 1 in photoperiod-influenced responses to ozone using Arabidopsis knockout mutants.
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Oxidative stress caused by ozone (O3 ) affects plant development, but the roles of specific redox-homeostatic enzymes in O3 responses are still unclear. While growth day length may affect oxidative stress outcomes, the potential influence of day length context on equal-time exposures to O3 is not
Glutathione reductase 2 maintains the function of photosystem II in Arabidopsis under excess light.
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Glutathione reductase plays a crucial role in the elimination of H(2)O(2) molecules via the ascorbate-glutathione cycle. In this study, we used transgenic Arabidopsis plants with decreased glutathione reductase 2 (GR2) levels to investigate whether this GR2 activity protects the photosynthetic
Genome-wide analysis of glutathione reductase (GR) genes from rice and Arabidopsis.
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Plant cells and tissues remain always on risk under abiotic and biotic stresses due to increased production of reactive oxygen species (ROS). Plants protect themselves against ROS induced oxidative damage by the upregulation of antioxidant machinery. Out of many components of antioxidant machinery,
The NADPH-dependent thioredoxin system constitutes a functional backup for cytosolic glutathione reductase in Arabidopsis.
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Tight control of cellular redox homeostasis is essential for protection against oxidative damage and for maintenance of normal metabolism as well as redox signaling events. Under oxidative stress conditions, the tripeptide glutathione can switch from its reduced form (GSH) to oxidized glutathione
High level of reduced glutathione contributes to detoxification of lipid peroxide-derived reactive carbonyl species in transgenic Arabidopsis overexpressing glutathione reductase under aluminum stress.
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Lipid peroxide-derived reactive carbonyl species (RCS), generated downstream of reactive oxygen species (ROS), are critical damage-inducing species in plant aluminum (Al) toxicity. In mammals, RCS are scavenged primarily by glutathione (reduced form of glutathione, GSH), but in plant Al stress,
Arabidopsis glutathione reductase 1 is dually targeted to peroxisomes and the cytosol.
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Plastid-localized glutathione reductase2-regulated glutathione redox status is essential for Arabidopsis root apical meristem maintenance.
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Glutathione is involved in thiol redox signaling and acts as a major redox buffer against reactive oxygen species, helping to maintain a reducing environment in vivo. Glutathione reductase (GR) catalyzes the reduction of glutathione disulfide (GSSG) into reduced glutathione (GSH). The Arabidopsis
Differential accumulation of antioxidant mRNAs in Arabidopsis thaliana exposed to ozone.
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Antioxidant isoenzymes function to eliminate free radicals and are localized to several different subcellular compartments within the plant cell. In Arabidopsis thaliana exposed to ozone (O3), we have monitored the accumulation of mRNAs encoding both cytosolic and chloroplastic antioxidant
Isolation of an abscisic acid senescence and ripening inducible gene from litchi and functional characterization under water stress.
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A full-length abscisic acid (ABA) senescence and ripening inducible gene named LcAsr was obtained from litchi. Bioinformatic analysis showed that full-length LcAsr was 1,177 bp and contained an open reading frame (ORF) encoding 153 amino acids, 85- and 146-bp 5' and 3' UTRs, respectively. LcAsr was
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