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Identification and expression analysis of NADH-cytochrome b(5) reductase gene in the cotton bollworm, Helicoverpa armigera

文献类型: 外文期刊

作者: Zhao, Chunqing 1 ; Tang, Tao 1 ; Liu, Jiqin 3 ; Feng, Xiaoyun 1 ; Qiu, Lihong 1 ;

作者机构: 1.China Agr Univ, Coll Sci, Beijing 100193, Peoples R China

2.Hunan Acad Agr Sci, Inst Plant Protect, Changsha, Hunan, Peoples R China

3.China Agr Univ, State Key Lab Agrobiotechnol, Dept Plant Pathol, Beijing 100193, Peoples R China

关键词: Helicoverpa armigera;NADH-cytochrome b(5) reductase (CBR);Cytochrome P450 enzyme systems (P450s);Phenobarbital (PB);Induction

期刊名称:GENE ( 影响因子:3.688; 五年影响因子:3.329 )

ISSN: 0378-1119

年卷期: 2012 年 511 卷 1 期

页码:

收录情况: SCI

摘要: NADH-cytochrome b(5) reductase (CBR) is one of the most important components of cytochrome P450s, which play an essential role in the detoxification of xenobiotics as well as insecticide resistance in insect pest. In the present study, two novel full-length cDNAs of CBR of the cotton bollworm, Helicoverpa armigera (Hubner) were amplified by means of reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends (RACE) techniques. The sequencing results showed that the transcripts were 1809 bp and 1518 bp for HaCBR1 and HaCBR2, respectively, including 969 bp and 939 bp of complete open reading frame (ORF), which encoded 322 and 312 amino acids respectively. The putative structure and function of HaCBR1 and HaCBR2 were preliminarily analyzed by SMART program. HaCBR1 and HaCBR2 (GenBank accession numbers: HQ638220 and HQ190046) showed high identities with CBRs of other species. The expression of HaCBR1 and HaCBR2 mRNA was detected by real-time quantitative polymerase chain reaction (RT-qPCR) in most developmental stages of H. armigera with the exception of eggs, as well as in tissues such as cuticle, fatbody and midgut. The expression level of the two genes was significantly induced by phenobarbital (PB). These results would contribute to the understanding of CBR function in H. armigera and provide information for further study on the interactions of different components of cytochrome P450 enzyme systems. (C) 2012 Elsevier B.V All rights reserved.

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