Characterization of an omega‐class glutathione S‐transferase in the stress response of the silkmoth
Characterization of an omega‐class glutathione S‐transferase in the stress response of the silkmoth
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DOI：
10.1111/j.1365-2583.2011.01073.x
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发表时间：
2011-06
影响因子：
2.6
通讯作者：
Kohji Yamamoto;S. Teshiba;Y. Shigeoka;Y. Aso;Y. Banno;T. Fujiki;Y. Katakura
中科院分区：
文献类型：
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作者：
Kohji Yamamoto;S. Teshiba;Y. Shigeoka;Y. Aso;Y. Banno;T. Fujiki;Y. Katakura
谷胱甘肽S-转移酶（GST）超家族参与各种外源性物质的解毒。使用真实的-时间PCR，显示在暴露于各种环境胁迫后诱导编码家蚕ω-类GST（bmGSTO）的mRNA。可溶性形式的重组蛋白（rbmGSTO）在大肠杆菌细胞中功能性过表达并纯化至均一。发现Cys 38和Pro 39在omega类GST中高度保守，并通过定点突变/动力学分析研究了它们的作用。Cys 38和Pro 39残基的突变影响酶的催化效率，表明Cys 38和Pro 39残基的存在对于bmGSTO活性是重要的。因此，bmGSTO可能有助于提高鳞翅目昆虫的环境胁迫抗性。
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.