Purification and Characterization of Corn Glutathione S-Transferase

Mozer, Thomas J.; Tiemeier, David C.; Jaworski, Ernest G.

doi:10.1016/b978-0-12-221480-6.50079-7

Cited by 22 publications

(42 citation statements)

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“…As with the multiple GSTs found in animal species, plant GSTs may be constitutively expressed and induced by external stimuli. Constitutive GSTs have been identified in several plant species including maize (GST III) [22,23], sugarcane [29] and Silene cucubalus [ 16]. In addition to these constitutively expressed isoforms, differential screening techniques have been used to isolate a number of inducible cDNA clones, which share significant homology with known GSTs.…”

Section: Introductionmentioning

confidence: 99%

“…The best characterised plant GST system occurs in maize, where they comprise 1-2~o of soluble protein [7,12,22]. Using a variety of substrates, anion exchange chromatography has been used to demonstrate a complex profile of GST isoforms in maize seedlings [4].…”

Section: Introductionmentioning

confidence: 99%

“…Four isoforms have been characterized in some detail. GST I and GST III are homodimers of 29 kDa and 26 kDa subunits respectively [22,31 ]. Both isoforms are constitutively expressed, however GST I m R N A levels can be elevated three to four fold in etiolated seedlings by herbicide safener treatment [32].…”

Section: Introductionmentioning

confidence: 99%

“…G S T I1 has been purified to homogeneity and has been shown to be a heterodimer composed of 29 kDa (GST-29) and 27 kDa (GST-27) subunits [12,22]. The ability of GST II to conjugate glutathione to a range of substrates, including chloroacetanilide herbicides (alachlor) and the non-herbicide substrate 1-chloro-2,4-dinitrobenzene (CDNB), has been reported [12].…”

Section: Introductionmentioning

confidence: 99%

“…The ability of GST II to conjugate glutathione to a range of substrates, including chloroacetanilide herbicides (alachlor) and the non-herbicide substrate 1-chloro-2,4-dinitrobenzene (CDNB), has been reported [12]. The 29 kDa subunit of GST II has been shown to be identical to the 29 kDa subunit present in GST I using N-terminal sequencing [22]. We have previously described how specific polyclonal antisera to the 27 kDa and 29 kDa subunits of GST II have been raised in sheep [ 12].…”

Section: Introductionmentioning

confidence: 99%

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Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV

Jepson¹,

Lay²,

Holt³

et al. 1994

Plant Mol Biol

131

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Several GSTs have been characterised in maize. GST I is a homodimer of 29 kDa subunits, GST II a hetrodimer of 27 kDa and 29 kDa subunits and GST IV a homodimer of 27 kDa subunits. We report the isolation and characterization of a herbicide-safener inducible cDNA clone, GST-27. Based on partial amino acid sequence, GST-27 encodes the 27 kDa subunit present in both glutathione S-transferase isoforms GST II and IV. Northern blotting was used to compare the expression patterns of GST-27 with that of GST-29. Transcripts corresponding to GST-27 were found to be constitutively expressed in RNA isolated from the root, but no expression was detected in RNA isolated from aerial parts of the plant. The application of herbicide safener caused a dramatic increase in the expression of GST-27 in all aerial plant parts tested. GST-29 was found to be constitutively expressed in RNA isolated from a number of maize tissues. The basal level of GST-29 expression showed a minimal increase upon herbicide safener treatment. Although a range of hormonal, environmental and physiological stimuli failed to elevate GST-27 levels, some increase in GST-27 mRNA was observed in the late stages of leaf senescence and after treatments resulting in phytotoxic effects.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV

Jepson¹,

Lay²,

Holt³

et al. 1994

Plant Mol Biol

131

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Characterisation of Multiple Glutathione Transferases Containing the GST I Subunit with Activities toward Herbicide Substrates in Maize (Zea mays)

Dixon

Cole²,

Edwards

1997

Pestic. Sci.

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The glutathione transferases (GSTs) of maize with activities toward chloroacetanilide herbicides are relatively well characterised, but their range of substrate speciÐcities has not been determined in detail. GST activities toward an extensive range of chemically diverse xenobiotic substrates, including the herbicides atrazine, alachlor, metolachlor and Ñuorodifen, have been determined in crude and puriÐed preparations from the roots and shoots of dark-grown maize seedlings treated with and without the herbicide-safener dichlormid. With the exception of the activity toward atrazine, speciÐc activities were higher in the roots than in the shoots in all cases. In untreated shoots activities were in the order atrazine \ alachlor \ metolachlor [ Ñuorodifen with safenerÈtreatment selectively increasing the activity toward the chloroacetanilides and Ñuorodifen. In the roots the highest GST activities toward herbicides were toward the chloroacetanilides. Dichlormid treatment resulted in an increase in activities toward all four herbicides in the roots of one maize cultivar (Pioneer 3394) but only enhanced the activities toward the chloroacetanilides and Ñuorodifen in cultivar Artus. Using the non-herbicide 1-chloro-2,4-dinitrobenzene (CDNB) as substrate, anion-exchange chromatography showed that the roots and shoots contained a similar range of GST isoenzymes. All of these isoenzymes were enhanced in response to safeners, though the extent of this induction was organdependent. GST isoenzymes containing the GST I subunit were puriÐed from safener-treated roots by a combination of hydrophobic interaction chromatography and affinity chromatography using Orange A agarose. Three isoenzymes could then be puriÐed following resolution by anion-exchange chromatography. The three GSTs were termed GST I/I, GST I/II and GST I/III with GST I, II and III referring to the presence of 29 kDa, 27 kDa and 26 kDa subunits respectively. This revised nomenclature for the maize GSTs was considered necessary in view of the continued discovery of new isoenzymes, such as GST I/III, composed of subunits which have been previously described. GST I/I had measurable activity toward atrazine, low activities toward the other herbicides and appreciable activities toward a range of other xenobiotic substrates. GST I/II and the novel GST I/III isoenzymes both showed high activities toward the chloroacetanilides and Ñuorodifen but lower activities toward the other substrates and negligible activities toward atrazine. The GST II subunit of GST I/II also had activity as a glutathione peroxidase. Our results show that the GST I subunit can form dimers with the GST III subunit in addition to the GST I and GST II subunits and that the degree of speciÐcity toward herbicide substrates of the respective isoenzymes is greater than previously reported. Our results also suggest that the safener-inducible GST II subunit has additional activities as a glutathione peroxidase.

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Pentachlorophenol: Uptake/elimination kinetics and metabolism in an aquatic plant, Eichhornia Crassipes

Roy

Hänninen

1994

Enviro Toxic and Chemistry

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Eichhornia crassipes [(Mart) Solms], an aquatic plant widely used for the treatment of wastewaters, was used to study uptake/elimination kinetics and metabolism of pentachlorophenol (PCP). PCP is a well‐known industrial by‐product and a major pollutant of the aquatic environment. The initial phase of PCP uptake by the plant was rapid and reached a nearly steady state between 24 and 48 h of exposure to PCP. The major by‐products of PCP metabolism in Eichhornia crassipes were identified as ortho‐ and para‐ substituted chlorohydroxyphenols (chlorocatechols and ‐hydroquinones), ‐anisoles, and ‐veratroles. Partially dechlorinated products of PCP were also detected. A major portion of the absorbed PCP and metabolites was found in bound/conjugated form. The responses of the enzyme systems involved in the xenobiotic metabolism and antioxidative system were also studied following PCP exposure. A significant increase was observed in the activity of glutathione S‐transferase (GST), a major conjugating enzyme, and in the activities of superoxide dismutase and ascorbate peroxidase (Halliwell‐Asada pathway enzymes) of PCP exposed plants. Such responses of plant enzymes may be implemented as useful markers of aquatic pollution. The result related to the uptake and metabolism of PCP obtained from the present study suggests a crucial role of aquatic plants in determining the fate of environmental chemicals.

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Purification and Characterization of Corn Glutathione S-Transferase

Cited by 22 publications

References 0 publications

Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV

Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV

Characterisation of Multiple Glutathione Transferases Containing the GST I Subunit with Activities toward Herbicide Substrates in Maize (Zea mays)

Pentachlorophenol: Uptake/elimination kinetics and metabolism in an aquatic plant, Eichhornia Crassipes

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