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Research article

Cloning, expression and biochemical characterization of one Epsilon-class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the Epsilon class

Rafał SAWICKI, Sharda P. SINGH, Ashis K. MONDAL, Helen BENEŠ, Piotr ZIMNIAK
Biochemical Journal Mar 01, 2003, 370 (2) 661-669; DOI: 10.1042/bj20021287
Rafał SAWICKI
Department of Medicine, University of Arkansas for Medical Sciences, Little Rock, AR 72205, U.S.A.
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Sharda P. SINGH
Department of Medicine, University of Arkansas for Medical Sciences, Little Rock, AR 72205, U.S.A.
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Ashis K. MONDAL
Department of Medicine, University of Arkansas for Medical Sciences, Little Rock, AR 72205, U.S.A.
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Helen BENEŠ
Department of Anatomy and Neurobiology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, U.S.A.
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Piotr ZIMNIAK
Department of Medicine, University of Arkansas for Medical Sciences, Little Rock, AR 72205, U.S.A.Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, U.S.A.,Central Arkansas Veterans Healthcare System, Medical Research (151/LR), 4300 West 7th Street, Little Rock, AR 72205, U.S.A.
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Abstract

From the fruitfly, Drosophila melanogaster, ten members of the cluster of Delta-class glutathione S-transferases (GSTs; formerly denoted as Class I GSTs) and one member of the Epsilon-class cluster (formerly GST-3) have been cloned, expressed in Escherichia coli, and their catalytic properties have been determined. In addition, nine more members of the Epsilon cluster have been identified through bioinformatic analysis but not further characterized. Of the 11 expressed enzymes, seven accepted the lipid peroxidation product 4-hydroxynonenal as substrate, and nine were active in glutathione conjugation of 1-chloro-2,4-dinitrobenzene. Since the enzymically active proteins included the gene products of DmGSTD3 and DmGSTD7 which were previously deemed to be pseudogenes, we investigated them further and determined that both genes are transcribed in Drosophila. Thus our present results indicate that DmGSTD3 and DmGSTD7 are probably functional genes. The existence and multiplicity of insect GSTs capable of conjugating 4-hydroxynonenal, in some cases with catalytic efficiencies approaching those of mammalian GSTs highly specialized for this function, indicates that metabolism of products of lipid peroxidation is a highly conserved biochemical pathway with probable detoxification as well as regulatory functions.

  • detoxification
  • Diptera
  • electrophile
  • glutathione conjugation
  • lipid peroxidation

Footnotes

  • Abbreviations used: CDNB, 1-chloro-2,4-dinitrobenzene; EST, expressed sequence tag; GST, glutathione S-transferase; 4-HNE, 4-hydroxynonenal; ORF, open reading frame; poly(A)+, polyadenylated; ROS, reactive oxygen species; RT, reverse transcriptase.

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March 2003

Volume: 370 Issue: 2

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Cloning, expression and biochemical characterization of one Epsilon-class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the Epsilon class
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Cloning, expression and biochemical characterization of one Epsilon-class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the Epsilon class
Rafał SAWICKI, Sharda P. SINGH, Ashis K. MONDAL, Helen BENEŠ, Piotr ZIMNIAK
Biochemical Journal Mar 2003, 370 (2) 661-669; DOI: 10.1042/bj20021287
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Cloning, expression and biochemical characterization of one Epsilon-class (GST-3) and ten Delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the Epsilon class
Rafał SAWICKI, Sharda P. SINGH, Ashis K. MONDAL, Helen BENEŠ, Piotr ZIMNIAK
Biochemical Journal Mar 2003, 370 (2) 661-669; DOI: 10.1042/bj20021287

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Keywords

detoxification
Diptera
electrophile
glutathione conjugation
lipid peroxidation

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