Biochemical properties of an omega-class glutathione S-transferase of the silkmoth, Bombyx mori.
A cDNA encoding an omega-class glutathione S-transferase of the silkmoth, Bombyx mori (bmGSTO), was cloned by reverse transcriptase-polymerase chain reaction. The resulting clone was sequenced and deduced for amino acid sequence, which revealed 40, 40, and 39% identities to omega-class GSTs from human, pig, and mouse, respectively. A recombinant protein (rbmGSTO) was functionally overexpressed in Escherichia coli cells in a soluble form and purified to homogeneity. rbmGSTO was able to catalyze the biotranslation of glutathione with 1-chloro-2,4-dinitrobenzene, a model substrate for GST, as well as with 4-hydroxynonenal, a product of lipid peroxidation. This enzyme was shown to have high affinity for organophosphorus insecticide and was present abundantly in silkmoth strain exhibiting fenitrothion resistance. These results indicate that bmGSTO could be involved in the increase in level of insecticide resistance for lepidopteran insects.
Yamamoto
Kohji
K
Institute of Genetic Resources, Faculty of Agriculture, Kyushu University Graduate School, Higashi-ku, Fukuoka 812-8581, Japan. yamamok@agr.kyushu-u.ac.jp
Nagaoka
Sumiharu
S
Banno
Yutaka
Y
Aso
Yoichi
Y
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000201:enzymology*; D003001:Cloning, Molecular; D005278:Fenitrothion / Q000633:toxicity; D005982:Glutathione Transferase / Q000737:chemistry*; D006801:Humans; D007928:Lethal Dose 50; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment
D005982:Glutathione Transferase; D005278:Fenitrothion