Characterization of an omega-class glutathione S-transferase in the stress response of the silkmoth

Kohji Yamamoto; S. Teshiba; Y. Shigeoka; Y. Aso; Yutaka Banno; T. Fujiki; Yoshinori Katakura

doi:10.1111/j.1365-2583.2011.01073.x

Characterization of an omega-class glutathione S-transferase in the stress response of the silkmoth

Kohji Yamamoto, S. Teshiba, Y. Shigeoka, Y. Aso, Yutaka Banno, T. Fujiki, Yoshinori Katakura

Systems Biology

Research output: Contribution to journal › Article › peer-review

26 Citations (Scopus)

Abstract

The glutathione S-transferase (GST) superfamily is involved in detoxification of various xenobiotics. Using real-time PCR, mRNA encoding an omega-class GST of Bombyx mori (bmGSTO) was shown to be induced after exposure to various environmental stresses. A soluble form of recombinant protein (rbmGSTO) was functionally overexpressed in Escherichia coli cells and purified to homogeneity.Cys 38 and Pro 39 were found to be highly conserved in omega-class GSTs, and their roles were investigated by site-directed mutagenesis/kinetic analysis. Mutations of Cys 38 and Pro 39 residues affected the catalytic efficiency of enzymes, indicating that the presence of Cys 38 and Pro 39 residues is important for bmGSTO activity. Thus, bmGSTO could contribute to increasing the environmental stress resistance of lepidopteran insects.

Original language	English
Pages (from-to)	379-386
Number of pages	8
Journal	Insect Molecular Biology
Volume	20
Issue number	3
DOIs	https://doi.org/10.1111/j.1365-2583.2011.01073.x
Publication status	Published - Jun 1 2011

All Science Journal Classification (ASJC) codes

Molecular Biology
Genetics
Insect Science

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abstract = "The glutathione S-transferase (GST) superfamily is involved in detoxification of various xenobiotics. Using real-time PCR, mRNA encoding an omega-class GST of Bombyx mori (bmGSTO) was shown to be induced after exposure to various environmental stresses. A soluble form of recombinant protein (rbmGSTO) was functionally overexpressed in Escherichia coli cells and purified to homogeneity.Cys 38 and Pro 39 were found to be highly conserved in omega-class GSTs, and their roles were investigated by site-directed mutagenesis/kinetic analysis. Mutations of Cys 38 and Pro 39 residues affected the catalytic efficiency of enzymes, indicating that the presence of Cys 38 and Pro 39 residues is important for bmGSTO activity. Thus, bmGSTO could contribute to increasing the environmental stress resistance of lepidopteran insects.",

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AU - Yamamoto, Kohji

AU - Teshiba, S.

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AU - Aso, Y.

AU - Banno, Yutaka

AU - Fujiki, T.

AU - Katakura, Yoshinori

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