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Characteristics and roles of cytochrome b(5) in cytochrome P450-mediated oxidative reactions in Locusta migratoria

文献类型: 外文期刊

作者: Liu Jiao 1 ; Zhang Xue-yao 1 ; Wu Hai-hua 1 ; Ma Wen 3 ; Zhu Wen-ya 4 ; Zhu, Kun-Yan 5 ; Ma En-bo 1 ; Zhang Jian-zhe 1 ;

作者机构: 1.Shanxi Univ, Inst Appl Biol, Taiyuan 030006, Peoples R China

2.Shanxi Univ, Coll Life Sci, Taiyuan 030006, Peoples R China

3.Shanxi Univ, Modern Res Ctr Tradit Chinese Med, Taiyuan 030006, Peoples R China

4.Shanxi Acad Agr Sci, Inst Plant Protect, Taiyuan 030031, Peoples R China

5.Kansas State Univ, Dept Entomol, Manhattan, KS 66506 USA

关键词: cytochrome b(5); cytochrome P450; cytochrome P450 reductase; Locusta migratoria; RNA interference

期刊名称:JOURNAL OF INTEGRATIVE AGRICULTURE ( 影响因子:2.848; 五年影响因子:2.979 )

ISSN: 2095-3119

年卷期: 2020 年 19 卷 6 期

页码:

收录情况: SCI

摘要: Cytochrome b(5) (Cyt-b(5)) is a small heme protein and known to be involved in a wide range of biochemical transformations, including cytochrome P450 monooxygenase (CYP)-mediated metabolism of endogenous and exogenous compounds. Studies on Cyt-b(5) are more concentrated in mammals, but are relatively rare in insects. The characteristics and function of Cyt-b(5) from Locusta migratoria have not been described yet. We sequenced the full-length cDNA sequence of Cyt-b(5) from L. migratoria (LmCyt-b(5)) by reverse transcription-PCR (RT-PCR) based on locust transcriptome database. The phylogenetic analysis showed that LmCyt-b(5) was closely related to the Cyt-b(5) from Blattodea. LmCyt-b(5) was highly expressed in ovary, Malpighian tubules, midgut, gastric caeca, and fat bodies. Silencing of LmCyt-b(5) had no effect on the susceptibility of L. migratoria to four different insecticides. Suppression of LmCyt-b(5) or silencing of both LmCyt-b(5) and LmCPR did not significantly change the total CYP activity toward the substrate 7-ethoxycoumarin (7-EC). However, coexpression of LmCYP6FD1 with LmCPR and LmCyt-b(5) together in Sf9 cells by using Bac-to-Bac baculovirus expression system significantly increased the catalytic activity of LmCYP6FD1 toward 7-EC as compared with the coexpression of LmCYP6FD1 with cytochrome P450 reductase (LmCPR) or LmCyt-b(5) separately. These results suggest that LmCyt-b(5) plays an important role in the catalytic reaction of LmCYP6FD1 toward 7-EC in our in vitro experiments. Further study is needed to clarify the role of LmCyt-b(5) in CYP-mediated catalytic reactions in L. migratoria.

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