International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
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Cloning and Characterization of Bombyx mori Cyclophilin A

  • Kim, Sung-Wan (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Yun, Eun-Young (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Kim, Seong-Ryul (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Park, Seung-Won (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Kang, Seok-Woo (Department of Agricultural Biology, National Academy of Agricultural Science, RDA) ;
  • Kwon, O-Yu (Department of Anatomy, College of Medicine, Chungnam National University) ;
  • Goo, Tae-Won (Department of Agricultural Biology, National Academy of Agricultural Science, RDA)
  • Received : 2011.09.22
  • Accepted : 2011.11.19
  • Published : 2011.12.31
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Abstract

Cyclophilins are originally identified as cytosolic binding protein of the immunosuppressive drug cyclosporine A. They have an activity of peptidyl prolyl cis/trans-isomerases (PPIase), which may play important roles in protein folding, trafficking, assembly and cell signaling. In this study, we report the cloning and characterization of a Bombyx mori cyclophilin A (bCypA) cDNA. The full-length cDNA of bCypA consist of 947 nucleotides with a polyadenylation signal sequence AATAAA and contain an open reading frame of 498 nucleotides encoding a polypeptide of 166 amino acids. The deduced amino acid sequence of bCypA shares a central peptidyl prolyl cis/trans-isomerase and a cyclosporin-A-binding domain with other cyclophilin sequences. Relative quantification real-time (RT) PCR analysis shows that mRNA transcripts of bCypA are detected in all the investigated tissues and highest expression level in the skin of 3-day-old 5 instar larva. Also, bCypA had PPIase activity on the proline-containing peptides. Accordingly, we suggest that bCypA is a new member of the cyclophilin A (CyPA) family and will be useful for quality control of bioactivity recombinant proteins with proline-containing peptides.

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