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 | |
| Publication status | Published - Jun 1 2011 |
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All Science Journal Classification (ASJC) codes
- Molecular Biology
- Genetics
- Insect Science
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Characterization of an omega-class glutathione S-transferase in the stress response of the silkmoth. / Yamamoto, Kohji; Teshiba, S.; Shigeoka, Y.; Aso, Y.; Banno, Yutaka; Fujiki, T.; Katakura, Yoshinori.
In: Insect Molecular Biology, Vol. 20, No. 3, 01.06.2011, p. 379-386.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of an omega-class glutathione S-transferase in the stress response of the silkmoth
AU - Yamamoto, Kohji
AU - Teshiba, S.
AU - Shigeoka, Y.
AU - Aso, Y.
AU - Banno, Yutaka
AU - Fujiki, T.
AU - Katakura, Yoshinori
PY - 2011/6/1
Y1 - 2011/6/1
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=79955738643&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2583.2011.01073.x
DO - 10.1111/j.1365-2583.2011.01073.x
M3 - Article
C2 - 21435060
AN - SCOPUS:79955738643
VL - 20
SP - 379
EP - 386
JO - Insect Molecular Biology
JF - Insect Molecular Biology
SN - 0962-1075
IS - 3
ER -