›› 2011, Vol. 54 ›› Issue (1): 1-8.doi:

• RESEARCH PAPERS •     Next Articles

Cloning, expression anaylsis and subcellular localization of P450 gene CYP6AE21 from Bombyx mori

WANG Dong, LI Bing, LIN Chao, CHEN Yu-Hua, XU Ya-Xiang, SHEN Wei-De   

  • Online:2011-01-20 Published:2011-01-20
  • About author:210316001@suda.edu.cn

Abstract: Signal inactivation is a critical step in the olfactory dynamic process, in which various odorant-degrading enzymes are involved. In this study, the cDNA of a cytochrome P450 gene, CYP6AE21, was cloned from the male moth antenna of Bombyx mori by RT-PCR method. CYP6AE21 contains a 1 572 bp open reading frame (ORF), which encodes a putative protein of 523 amino acids. This cDNA-deduced protein has a predicted molecular weight (MW) of 60.5 kD, isoelectric point (pI) of 8.4, and a P450 characteristic structure heme-binding region. A single intron is localized at the same site in each of the P450 gene CYP6AE21 and CYP6AE2 from B. mori, and two corresponding exons with the same size exist in both of the genes. The two genes share 94.5% nucleotide similarity, and cluster on the same chromosome in a head-to-tail arrangement separated by an approximately 7.6 kb intergenic region. CYP6AE21 was highly expressed in larval head and fat body, and both male and female moth antenna. It was also expressed in other tissues of larvae and some tissues of moth. NADPH cytochrome P450 reductase (CPR), a very important component of monooxygenase system, was also highly expressed in the moth antenna, and expressed in other moth tissues at low levels. Subcellular localization analysis showed that the expression product of CYP6AE21 is localized in cytoplasm. It is so inferred that CYP6AE21 and CYP6AE2 could have been formed by gene duplication of either of them, and CYP6AE21 might participate in the degradation of odorants after these components are internalized into cells.

Key words: Bombyx mori, cytochrome P450, CYP6 family, subcellular localization, olfaction, odorant degrading enzyme