An omega-class glutathione S-transferase in the brown planthopper Nilaparvata lugens exhibits glutathione transferase and dehydroascorbate reductase activities
An omega-class glutathione S-transferase in the brown planthopper Nilaparvata lugens exhibits glutathione transferase and dehydroascorbate reductase activities
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DOI：
10.1002/arch.21599
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发表时间：
2019-07-22
影响因子：
2.2
通讯作者：
Yamamoto, Kohji
中科院分区：
文献类型：
--
作者：
Saruta, Fumiko;Yamada, Naotaka;Yamamoto, Kohji
利用反转录聚合酶链反应（RT-PCR）技术，从褐飞虱（Nilaparvata lugens）中分离到一个编码ω-谷胱甘肽S-转移酶（GST）的互补DNA。通过在大肠杆菌细胞中过表达获得重组蛋白（nlGSTO）并纯化。nIGSTO催化谷胱甘肽与GST的一般底物1-氯-2，4-二硝基苯以及脱氢抗坏血酸的生物转化以合成抗坏血酸。突变实验表明，推定的底物结合位点，包括Phe28，Cys29，Phe30，Arg176，和Lue225，谷胱甘肽转移酶和脱氢抗坏血酸还原酶的活动是重要的。由于抗坏血酸是还原剂，nIGSTO可能参与抗氧化剂抗性。
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.