An omega-class glutathione S-transferase in the brown planthopper Nilaparvata lugens exhibits glutathione transferase and dehydroascorbate reductase activities

Fumiko Saruta, Naotaka Yamada, Kohji Yamamoto

Research output: Contribution to journalArticle

Abstract

A complementary DNA that encodes an omega-class glutathione S-transferase (GST) of the brown planthopper, Nilaparvata lugens (nlGSTO), was isolated by reverse transcriptase polymerase chain reaction. A recombinant protein (nlGSTO) was obtained via overexpression in the Escherichia coli cells and purified. nlGSTO catalyzes the biotransformation of glutathione with 1-chloro-2,4-dinitrobenzene, a general substrate for GST, as well as with dehydroascorbate to synthesize ascorbate. Mutation experiments revealed that putative substrate-binding sites, including Phe28, Cys29, Phe30, Arg176, and Lue225, were important for glutathione transferase and dehydroascorbate reductase activities. As ascorbate is a reducing agent, nlGSTO may participate in antioxidant resistance.

Original languageEnglish
Article numbere21599
JournalArchives of insect biochemistry and physiology
Volume102
Issue number1
DOIs
Publication statusPublished - Jan 1 2019

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glutathione dehydrogenase (ascorbate)
Nilaparvata lugens
Glutathione Reductase
Glutathione Transferase
glutathione transferase
Dinitrochlorobenzene
complementary DNA
reducing agents
Polymerase chain reaction
RNA-Directed DNA Polymerase
Reducing Agents
Substrates
Biotransformation
biotransformation
Reverse Transcriptase Polymerase Chain Reaction
Recombinant Proteins
recombinant proteins
Escherichia coli
Glutathione
glutathione

All Science Journal Classification (ASJC) codes

  • Physiology
  • Biochemistry
  • Insect Science

Cite this

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abstract = "A complementary DNA that encodes an omega-class glutathione S-transferase (GST) of the brown planthopper, Nilaparvata lugens (nlGSTO), was isolated by reverse transcriptase polymerase chain reaction. A recombinant protein (nlGSTO) was obtained via overexpression in the Escherichia coli cells and purified. nlGSTO catalyzes the biotransformation of glutathione with 1-chloro-2,4-dinitrobenzene, a general substrate for GST, as well as with dehydroascorbate to synthesize ascorbate. Mutation experiments revealed that putative substrate-binding sites, including Phe28, Cys29, Phe30, Arg176, and Lue225, were important for glutathione transferase and dehydroascorbate reductase activities. As ascorbate is a reducing agent, nlGSTO may participate in antioxidant resistance.",
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