A Genomics Approach to the Comprehensive Analysis of the Glutathione <i>S</i>-Transferase Gene Family in Soybean and Maize

McGonigle, Brian; Keeler, Sharon J.; Lau, Sze-Mei Cindy; Koeppe, Mary K.; O’Keefe, Daniel P.

doi:10.1104/pp.124.3.1105

Cited by 281 publications

(291 citation statements)

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“…Fragments of the ORFs (gstI and gstIIIb), or fragments containing 3Ј UTRs joined to the 3Ј ends of the ORF (apx, StUCP, and TaUCP), were obtained by reverse transcriptase-mediated PCR with total RNA from normal maize seedlings as a template and were cloned into pGEMT-Easy. Although GSTI and GSTIIIb proteins are homologous (50% identity) and belong to the same family of maize GSTs (type I; McGonigle et al, 2000), there was no nucleotide homology detected for the gstI and gstIII PCR fragments used for analysis.…”

Section: Other Hybridization Probesmentioning

confidence: 99%

“…Maize orthologs of cytosolic glutathione S-transferases type I (gstI and gstIIIb; McGonigle et al, 2000) and ascorbate peroxidase (apx; Shigeoka et al, 2002) were chosen for analysis (Table 1). The maize gstIIIb and apx genes are related closely to Arabidopsis and tobacco genes that serve as markers for the oxidative burst response (Alvarez et al, 1998;Mittler et al, 1999).…”

Section: Analysis Of Oxidative Stress In Ncs Mutantsmentioning

confidence: 99%

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Differential Expression of Alternative Oxidase Genes in Maize Mitochondrial Mutants

et al. 2002

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We have examined the expression of three alternative oxidase ( aox ) genes in two types of maize mitochondrial mutants. Nonchromosomal stripe (NCS) mutants carry mitochondrial DNA deletions that affect subunits of respiratory complexes and show constitutively defective growth. Cytoplasmic male-sterile (CMS) mutants have mitochondrial DNA rearrangements, but they are impaired for mitochondrial function only during anther development. In contrast to normal plants, which have very low levels of AOX, NCS mutants exhibit high expression of aox genes in all nonphotosynthetic tissues tested. The expression pattern is specific for each type of mitochondrial lesion: the NADH dehydrogenase-defective NCS2 mutant has high expression of aox2 , whereas the cytochrome oxidase-defective NCS6 mutant predominantly expresses aox3 . Similarly, aox2 and aox3 can be induced differentially in normal maize seedlings by specific inhibitors of these two respiratory complexes. Translation-defective NCS4 plants show induction of both aox2 and aox3 . AOX2 and AOX3 proteins differ in their ability to be regulated by reversible dimerization. CMS mutants show relatively high levels of aox2 mRNAs in young tassels but none in ear shoots. Significant expression of aox1 is detected only in NCS and CMS tassels. The induction pattern of maize aox genes could serve as a selective marker for diverse mitochondrial defects.

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Section: Other Hybridization Probesmentioning

confidence: 99%

Section: Analysis Of Oxidative Stress In Ncs Mutantsmentioning

confidence: 99%

Differential Expression of Alternative Oxidase Genes in Maize Mitochondrial Mutants

et al. 2002

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“…55 GSTs in Arabidopsis thaliana (Dixon et al 2009), 82 in Oryza sativa , 81 in Populus (Lan et al 2009), 42 in maize (McGonigle et al 2000), 65 in broccoli (Vijayakumar et al 2016), 84 in Hordeum vulgare (Rezaei et al 2013), 20 in Draceana cambodiana (Zhu et al 2016), and 37 GSTs in Physcomitrella patens (a bryophyte) have been identified (Liu et al 2013). …”

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In silico genome-wide identification and characterization of the glutathione S-transferase gene family in Vigna radiata

Vaish

Awasthi

Tiwari

et al. 2018

Genome

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Plant glutathione S-transferases are integral to normal plant metabolism, and biotic and abiotic stress tolerance. GST gene family has been characterized in diverse plant species using molecular biology and bioinformatics approaches. In the current study, in silico analysis identified 44 GSTs in Vigna radiata. Of the total 44 GSTs identified, chromosomal locations of 31 GSTs were confirmed. The pI value of GST proteins ranged from 5.10 to 9.40. The predicted molecular weights ranged from 13.12 to 50 kDa. Subcellular localization analysis revealed that all GSTs were predominantly localized in the cytoplasm. The active site amino acids were confirmed to be serine in tau, phi, theta, zeta and TCHQD; cysteine in lambda, DHAR and omega; and tyrosine in EF1G. The gene architecture conformed to the 2 exon-1 intron and 3 exon-2 intron organization in case of tau and phi classes, respectively. MEME analysis identified 10 significantly conserved motifs with the width of 8 to 50 amino acids. The motifs identified were either specific to a specific GST class, or were shared by multiple GST classes. The results of the current study will be of potential importance in the characterization of GST gene family in V. radiata, an economically important leguminous crop.

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“…In plants, the glutathione transferases (GSTs 2 ; EC 2.5.1.18) are a superfamily of proteins with the dominant Phi (F) and Tau (U) classes having largely undefined functions in endogenous metabolism (1). This is in contrast to their relatively well studied role in catalyzing the glutathione conjugation of herbicides (2).…”

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confidence: 99%

Selective Binding of Glutathione Conjugates of Fatty Acid Derivatives by Plant Glutathione Transferases

Dixon

Edwards

2009

Journal of Biological Chemistry

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Proteomic studies with Arabidopsis thaliana have revealed that the plant-specific Tau (U) class glutathione transferases (GSTs) are selectively retained by S-hexylglutathione affinity supports. Overexpression of members of the Arabidopsis GST superfamily in Escherichia coli showed that 25 of the complement of 28 GSTUs caused the aberrant accumulation of acylated glutathione thioesters in vivo, a perturbation that was not observed with other GST classes. Each GSTU caused a specific group of fatty acyl derivatives to accumulate, which varied in chain length (C 6 to C 18 ), additional oxygen content (0 or 1), and desaturation (0 or 1). Thioesters bound tightly to recombinant GSTs (K d ϳ 1 M), explaining their accumulation. Transient expression of GSTUs in Nicotiana benthamiana followed by recovery by Strep-tag affinity chromatography allowed the respective plant ligands to be extracted and characterized. Again, each GST showed a distinct profile of recovered metabolites, notably glutathionylated oxophytodienoic acid and related oxygenated fatty acids. Similarly, the expression of the major Tau protein GSTU19 in the endogenous host Arabidopsis led to the selective binding of the glutathionylated oxophytodienoic acid-glutathione conjugate, with the enzyme able to catalyze the conjugation reaction. Additional ligands identified in planta included other fatty acid derivatives including divinyl ethers and glutathionylated chlorogenic acid. The strong and specific retention of various oxygenated fatty acids by each GSTU and the conservation in binding observed in the different hosts suggest that these proteins have selective roles in binding and conjugating these unstable metabolites in vivo.In plants, the glutathione transferases (GSTs 2 ; EC 2.5.1.18) are a superfamily of proteins with the dominant Phi (F) and Tau (U) classes having largely undefined functions in endogenous metabolism (1). This is in contrast to their relatively well studied role in catalyzing the glutathione conjugation of herbicides (2). Because of their importance in determining herbicide selectivity, these proteins have been purified from a range of major crops including maize (3), soybean (4), and wheat (5, 6). One approach which has been commonly applied to isolate these proteins is affinity chromatography using a range of glutathione (GSH) derivatives as ligands (7). These ligands often display a surprising degree of selectivity in capturing specific GSTs. Thus, in wheat extracts, whereas GSH-agarose effectively isolated GSTFs, S-hexylglutathione (GS-hexyl) proved to be a selective ligand for GSTUs (5). Similarly, glutathionylated dyes have proved to be highly selective for specific GSTs in maize (8).In each application, the use of GSH derivatives as affinity ligands has been developed through serendipity, with limited attention directed to the potential significance of such binding selectivity in relating to the nature of in vivo substrates and reaction products. At a molecular level, crystallographic studies with both plant GSTFs (9) and GSTUs...

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A Genomics Approach to the Comprehensive Analysis of the Glutathione S-Transferase Gene Family in Soybean and Maize

Cited by 281 publications

References 62 publications

Differential Expression of Alternative Oxidase Genes in Maize Mitochondrial Mutants

Differential Expression of Alternative Oxidase Genes in Maize Mitochondrial Mutants

In silico genome-wide identification and characterization of the glutathione S-transferase gene family in Vigna radiata

Selective Binding of Glutathione Conjugates of Fatty Acid Derivatives by Plant Glutathione Transferases

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