Alcohol dehydrogenase 5 of Helicoverpa armigera interacts with the CYP6B6 promoter in response to 2 ‐tridecanone

AbstractAlcohol dehydrogenase 5 (ADH5) is a member of medium ‐chain dehydrogenase/reductase family and takes part in cellular formaldehyde and S‐nitrosoglutathione metabolic network. 2‐tridecanone (2‐TD) is a toxic compound in manySolanaceae crops to defend against a variety of herbivory insects. In the broader context of insect development and pest control strategies, this study investigates how a new ADH5 fromHelicoverpa armigera (HaADH5) regulates the expression ofCYP6B6, a gene involved in molting and metamorphosis, in response to 2 ‐TD treatment. Cloning of theHaADH5 complementary DNA sequence revealed that its 1002 bp open reading frame encodes 334 amino acids with a predicted molecular weight of 36.5 kD.HaADH5 protein was purified in theEscherichia coli Transetta (pET32a ‐HaADH5) strain using a prokaryotic expression system. The ability ofHaADH5 protein to interact with the 2 ‐TD responsive region within the promoter ofCYP6B6 was confirmed by anin vitro electrophoretic mobility shift assay and transcription activity validation in yeast. Finally, the expression levels of bothHaADH5 andCYP6B6 were found to be significantly decreased in the midgut of 6th instar larvae after 48 h of treatment with 10 mg/g 2 ‐TD artificial diet. These results indicate that upon 2‐TD treatment of cotton bollworm,HaADH5 regulates the expression ofCYP6B6 by interacting with its promoter. AsHaADH5 regulation ofCYP6B6 expression may contribute to the larval xenobiotic detoxific...
Source: Insect Science - Category: Biology Authors: Tags: ORIGINAL ARTICLE Source Type: research