Plant Glutathione Peroxidase Research Articles

Comprehensive identification of glutathione peroxidase (GPX) gene family in response to abiotic stress in pepper (Capsicum annuum L.)

Plant glutathione peroxidase (GPX) plays an important role in the maintenance of cell homeostasis and in the antioxidant response in plants. In this study, the peroxidase (GPX) gene family was identified in the whole genome of pepper using bioinformatic method. As a result, a total of 5 CaGPX genes were identified, which were unevenly distributed on 3 of the 12 chromosomes of pepper genome. Based on phylogenetic analysis, 90 GPX genes in 17 species from lower plants to higher plants can be divided into 4 groups (GroupⅠ, Group Ⅱ, Group Ⅲ, Group Ⅳ). The MEME Suite analysis of GPX proteins shows that all these proteins contain four highly conserved motifs, as well as other conserved sequences and amino acid residues. Gene structure analysis revealed the conservative exon-intron organization pattern of these genes. In the promoter region of CaGPX genes, many cis elements of plant hormone and abiotic stress response were identified in each of CaGPX proteins. In addition, expression patterns of CaGPX genes in different tissues, developmental stages and responses to abiotic stress were also performed. The results of qRT-PCR showed that the transcripts of CaGPX genes varied greatly under abiotic stress at different time points. There results suggest that the GPX gene family of pepper may play a role in plant development andstress response. In conclusion, our research provides new insights into the evolution of pepper GPX gene family, and understanding for functional of these genes in response to abiotic stresses.

Identification and Characterization of the Glutathione Peroxidase (GPX) Gene Family in Watermelon and Its Expression under Various Abiotic Stresses

Plant glutathione peroxidase (GPX) is an important antioxidant enzyme to maintain H2O2 homeostasis and regulate plant response to abiotic stress. In this paper, we present the first report of a genome-wide identification of GPX genes in watermelon. A total of six genes (ClGPX1–ClGPX6) were identified, which were unevenly located on four chromosomes of the watermelon genome. Based on phylogenetic analysis, the GPX genes of Arabidopsis, rice, cucumber, and sorghum were classified into four groups. Through analyzing the promoter regions of ClGPX genes, many development-, stress-, and hormone-responsive cis-acting regulatory elements were also identified. Expression pattern analysis by qRT-PCR indicated that all ClGPX genes were actively expressed in flowers and fruits, and exhibited relatively lower expression in other tissues, particularly roots and stems. In addition, the expression of ClGPX genes was significantly induced by salt, drought, and cold stresses, as well as abscisic acid (ABA) treatment at different time points, suggesting that they may be involved in response to abiotic stress and ABA. Taken together, our findings demonstrated that ClGPX genes might function in watermelon development, especially in flower and fruit tissue, as well as in response to abiotic stress and hormones.

Molecular mechanism investigation on the interactions of copper (II) ions with glutathione peroxidase 6 from Arabidopsis thaliana

Accumulation of copper (II) ions in plant leads to the excessive reactive oxygen species (ROS) which attributes to the depletion of the antioxidants in the cell and destruction to antioxidant enzymes. The antioxidant enzyme glutathione peroxidase has been used as biomarkers to reflect metal-induced oxidative stress. However, the underlying toxic mechanisms of the copper ions(II)-induced oxidative damage to plants remain unknown. In the work, a detailed molecular interaction of copper (II) ions with Arabidopsis thaliana glutathione peroxidase 6 (AtGPX6) in relation with poisonous effects of exposure to heavy metal was investigated by multiple spectroscopic techniques. The intrinsic fluorescence of AtGPX6 was quenched upon the addition of copper (II) ions by the combination of static and dynamic quenching mechanisms accompanied by complex formation and conformational changes. A single binding site was revealed for AtGPX6 towards copper ions. The binding process was hydrophobic effect accompanied by positive entropy change and enthalpy change. The secondary structure of AtGPX6 was changed by the addition of copper ions investigated by synchronous fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy and circular dichroism spectroscopy, resulting in loosened and deconstructed protein skeleton and increased hydrophobicity around the Trp residues. This study helps to illuminate the detailed interactions between copper ions and plant glutathione peroxidase and elucidate the destructive mechanism to antioxidative defense system caused by heavy metal exposure at molecular level.

The Glutathione Peroxidase Gene Family in Gossypium hirsutum: Genome-Wide Identification, Classification, Gene Expression and Functional Analysis

The plant glutathione peroxidase (GPX) family consists of multiple isoenzymes with distinct subcellular locations, tissue-specific expression patterns and environmental stress responses. In this study, 13 putative GPXs from the genome of Gossypium hirsutum (GhGPXs) were identified and a conserved pattern among plant GPXs were exhibited, besides this they also responded to multiple environmental stresses and we predicted that they had hormone responsive cis-elements in their promoter regions. Most of the GhGPXs on expression in yeast can scavenge H2O2. Our results showed that different members of the GhGPX gene family were co-ordinately regulated under specific environmental stress conditions, and suggested the importance of GhGPXs in hormone treatments and abiotic stress responses.

A redox-dependent dimerization switch regulates activity and tolerance for reactive oxygen species of barley seed glutathione peroxidase

Monomeric and dimeric forms of recombinant barley (Hordeum vulgare subsp. vulgare) glutathione peroxidase 2 (HvGpx2) are demonstrated to display distinctly different functional properties in vitro. Monomeric HvGpx2 thus has five fold higher catalytic efficiency than the dimer towards tert-butyl hydroperoxide, but is more sensitive to inactivation by hydrogen peroxide. Treatment of the monomer with hydrogen peroxide results in dimer formation. This observed new behavior of a plant glutathione peroxidase suggests a mechanism involving a switch from a highly catalytically competent monomer to a less active, but more oxidation-resistant dimer.

Characterization and Analyses of Hydrophobic Clusters, Acetylation and Myristoylation Sites in Plant Glutathione Peroxidase Sequences

Incomplete reduction of oxygen molecules is the primary source for the formation of reactive oxygen species (ROS) during cytosolic metabolism or mitochondrial respiration. These phenomenons may be as a result of biotic or abiotic stress. Exposure to exogenous stimuli such as radiation might be an alternative pathway of ROS production. Thus plants require counter defense strategies to combat the increase of this toxic molecular build up in its cell cytoplasm. As a result they have devised an army of free radical scavenging enzymes which enable them to dissipate the oxidative stress imposed by the accumulation of these toxic moieties. Glutathione Peroxidase forms an important part of this arms race along with several catalases and organelle specific enzymes such as superoxide dismutase. Plant glutathione peroxidases (GPXs) have been studied exclusively for their evolutionary lineages since they represent a hybrid class of molecules in context of the presence and absence of selenocysteine at their catalytic centres, the former situation predominant in non vascular plant groups while the later a predominant feature of vascular plants. This analysis focuses on three important aspects of protein structure analyses – hydrophobic cluster analyses for identification of homologues, and acetylation and myristoylation sites which provide us with information regarding the post translational modifications of a particular protein group. Specific patterns of clusters along with acetylation and myristoylation site frequencies were obtained which indicate that GPXs of non vascular plant members possess less chances of getting myristoylated while acetylation was predominant in most land plant lineages but absent in aquatic members.

Characterization and Analyses of Hydrophobic Clusters, Acetylation and Myristoylation Sites in Plant Glutathione Peroxidase Sequences

Incomplete reduction of oxygen molecules is the primary source for the formation of reactive oxygen species (ROS) during cytosolic metabolism or mitochondrial respiration. These phenomenons may be as a result of biotic or abiotic stress. Exposure to exogenous stimuli such as radiation might be an alternative pathway of ROS production. Thus plants require counter defense strategies to combat the increase of this toxic molecular build up in its cell cytoplasm. As a result they have devised an army of free radical scavenging enzymes which enable them to dissipate the oxidative stress imposed by the accumulation of these toxic moieties. Glutathione Peroxidase forms an important part of this arms race along with several catalases and organelle specific enzymes such as superoxide dismutase. Plant glutathione peroxidases (GPXs) have been studied exclusively for their evolutionary lineages since they represent a hybrid class of molecules in context of the presence and absence of selenocysteine at their catalytic centres, the former situation predominant in non vascular plant groups while the later a predominant feature of vascular plants. This analysis focuses on three important aspects of protein structure analyses – hydrophobic cluster analyses for identification of homologues, and acetylation and myristoylation sites which provide us with information regarding the post translational modifications of a particular protein group. Specific patterns of clusters along with acetylation and myristoylation site frequencies were obtained which indicate that GPXs of non vascular plant members possess less chances of getting myristoylated while acetylation was predominant in most land plant lineages but absent in aquatic members.

Structural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidases.

TbTDPX (Trypanosoma brucei tryparedoxin-dependent peroxidase) is a genetically validated drug target in the fight against African sleeping sickness. Despite its similarity to members of the GPX (glutathione peroxidase) family, TbTDPX2 is functional as a monomer, lacks a selenocysteine residue and relies instead on peroxidatic and resolving cysteine residues for catalysis and uses tryparedoxin rather than glutathione as electron donor. Kinetic studies indicate a saturable Ping Pong mechanism, unlike selenium-dependent GPXs, which display infinite Km and Vmax values. The structure of the reduced enzyme at 2.1 Å (0.21 nm) resolution reveals that the catalytic thiol groups are widely separated [19 Å (0.19 nm)] and thus unable to form a disulphide bond without a large conformational change in the secondary-structure architecture, as reported for certain plant GPXs. A model of the oxidized enzyme structure is presented and the implications for small-molecule inhibition are discussed.

Immunolocalization of a plant glutathione peroxidase-like protein.

We report on the localization of GPXle-1, a plant glutathione peroxidase (GPX)-like protein, in the internode of Lycopersicon esculentum Mill. GPXle-1 was detected in the cytoplasm near to the plasma membrane of trichomes, in the wall of collenchyma and in both the cytoplasm and wall of vascular tissues. GPXle-1 was not found in the epidermis or parenchyma. After mechanical stimulation, a change in its cell distribution was recorded. In stimulated plants, GPXle-1 was detected throughout the cytoplasm in the epidermis, collenchyma and cortical parenchyma.

Molecular characterization of the glutathione peroxidase gene of the human malaria parasite Plasmodium falciparum

In this paper we report the isolation and the characterization of a gene encoding the antioxidant enzyme glutathione peroxidase from the human malaria parasite Plasmodium falciparum. This gene contains two introns of 208 and 168 bp and is present in a single copy on chromosome 13. The open reading frame encodes a protein with a predicted length of 205 amino acids, which possesses a potential cleavage site between residues 21 and 22 after a hydrophobic region with the characteristics of a signal sequence. Therefore, the mature protein is predicted to be 184 residues long with a molecular mass of 21 404 Da. In comparison with other known glutathione peroxidases many amino acid residues implicated in catalysis are conserved in the malarial enzyme. Phylogenetic analysis indicates that the deduced protein sequence is more closely related to plant glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase. A 1.5-kb transcript was identified in asynchronous erythrocytic stages.