Abstract
Two cDNAs encoding glutathione S-transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon-class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.
| Original language | English |
|---|---|
| Article number | e21443 |
| Journal | Archives of insect biochemistry and physiology |
| Volume | 97 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Mar 2018 |
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All Science Journal Classification (ASJC) codes
- Physiology
- Biochemistry
- Insect Science
Cite this
Enzymatic characterization of two epsilon-class glutathione S-transferases of Spodoptera litura. / Hirowatari, Aiko; Chen, Zhiwei; Mita, Kazuei; Yamamoto, Kohji.
In: Archives of insect biochemistry and physiology, Vol. 97, No. 3, e21443, 03.2018.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Enzymatic characterization of two epsilon-class glutathione S-transferases of Spodoptera litura
AU - Hirowatari, Aiko
AU - Chen, Zhiwei
AU - Mita, Kazuei
AU - Yamamoto, Kohji
PY - 2018/3
Y1 - 2018/3
N2 - Two cDNAs encoding glutathione S-transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon-class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.
AB - Two cDNAs encoding glutathione S-transferase (GST) of the tobacco cutworm, Spodoptera litura, were cloned by reverse transcriptase-polymerase chain reaction. The deduced amino acid sequences of the resulting clones revealed 32–51% identities to the epsilon-class GSTs from other organisms. The recombinant proteins were functionally overexpressed in Escherichia coli cells in soluble form and were purified to homogeneity. The enzymes were capable of catalyzing the bioconjugation of glutathione with 1-chloro-2,4-dinitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)-propane, and ethacrynic acid. A competition assay revealed that the GST activity was inhibited by insecticides, suggesting that it could be conducive to insecticide tolerance in the tobacco cutworm.
UR - http://www.scopus.com/inward/record.url?scp=85038035969&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85038035969&partnerID=8YFLogxK
U2 - 10.1002/arch.21443
DO - 10.1002/arch.21443
M3 - Article
C2 - 29235695
AN - SCOPUS:85038035969
VL - 97
JO - Archives of Insect Biochemistry and Physiology
JF - Archives of Insect Biochemistry and Physiology
SN - 0739-4462
IS - 3
M1 - e21443
ER -