Expression and characterization of a sigma-class glutathione S-transferase of the fall webworm, Hyphantria cunea

Kohji Yamamoto, Hiroshi Fujii, Yoichi Aso, Yutaka Banno, Katsumi Koga

Research output: Contribution to journalArticlepeer-review

57 Citations (Scopus)

Abstract

A cDNA encoding glutathione S-transferase (GST) of the fall webworm, Hyphantria cunea, was cloned by reverse transcriptase-polymerase chain reaction. The resulting clone (hcGST) was sequenced and deduced for amino acid sequence, which revealed 87, 59, and 42% identities to Sigma-class GSTs from Bombyx mori, Manduca sexta, and Blattella germanica respectively. A recombinant hcGST protein (rhcGST) was functionally overexpressed in Escherichia coli cells in a soluble form and purified to homogeneity. rhcGST retained more than 75% of its original GST activity after incubation at pHs 6 to 11. Incubation for 30 min at temperatures below 50°C scarcely affected the activity. rhcGST was able to catalyze the reaction of glutathione with 1- chloro-2,4-dinitrobenzene, a universal substrate for GST, as well as with 4-hydroxynonenal, a product of lipid peroxidation. We also found that as compared to B. mori Sigma-class GST, rhcGST had a higher affinity for fenitrothion, an organophosphorus insecticide.

Original languageEnglish
Pages (from-to)553-560
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Volume71
Issue number2
DOIs
Publication statusPublished - 2007

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Fingerprint

Dive into the research topics of 'Expression and characterization of a sigma-class glutathione S-transferase of the fall webworm, Hyphantria cunea'. Together they form a unique fingerprint.

Cite this