Cloning and Characterization of Bombyx mori Cyclophilin A

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 rep...

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Published in:International Journal of Industrial Entomology 2011, 23(2), , pp.223-229
Main Authors: Kim, S.W., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Yun, E.Y., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Kim, S.R., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Park, S.W., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Kang, S.W., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea, Kwon, O.Y., Chungnam National University, Daejeon, Republic of Korea, Goo, T.W., National Academy of Agricultural Science, RDA, Suwon, Republic of Korea
Format: Article
Language:English
Subjects:
BOMBYX MORI
Cyclophilin A
PPI
농학
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Summary: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.
ISSN:1598-3579
2586-4785
DOI:10.7852/ijie.2011.23.2.223