633
Views
56
CrossRef citations to date
0
Altmetric
Original Articles

A New Method for the Modification of Fibroin Heavy Chain Protein in the Transgenic Silkworm

, , , , , & show all
Pages 2943-2951 | Received 05 Jun 2007, Accepted 22 Aug 2007, Published online: 22 May 2014

  • 1) Kusuda, J., Tazima, Y., Onimaru, K., Ninaki, O., and Suzuki, Y., The sequence around the 5′ end of the fibroin gene from the wild silkworm, Bombyx mandarina, and comparison with that of the domesticated species, B. mori. Mol. Gen. Genet., 203, 359–364 (1986).
  • 2) Tanaka, K., and Mizuno, S., Homologues of fibroin L-chain and P25 of Bombyx mori are present in Dendrolimus spectabilis and Papilio xuthus but not detectable in Antheraea yamamai. Insect Biochem. Mol. Biol., 31, 665–677 (2001).
  • 3) Tanaka, K., Kajiyama, N., Ishikura, K., Waga, S., Kikuchi, A., Ohtomo, K., Takagi, T., and Mizuno, S., Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori. Biochim. Biophys. Acta, 1432, 92–103 (1999).
  • 4) Inoue, S., Tanaka, K., Arisaka, F., Kimura, S., Ohtomo, K., and Mizuno, S., Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio. J. Biol. Chem., 275, 40517–40528 (2000).
  • 5) Wang, S. P., Guo, T. Q., Guo, X. Y., Huang, J. T., and Lu, C. D., In vivo analysis of fibroin heavy chain signal peptide of silkworm Bombyx mori using recombinant baculovirus as vector. Biochem. Biophys. Res. Commun., 341, 1203–1210 (2006).
  • 6) Jin, H. J., and Kaplan, D. L., Mechanism of silk processing in insects and spiders. Nature, 424, 1057–1061 (2003).
  • 7) Tamura, T., Thibert, C., Royer, C., Kanda, T., Abraham, E., Kamba, M., Komoto, N., Thomas, J. L., Mauchamp, B., Chavancy, G., Shirk, P., Fraser, M., Prudhomme, J. C., and Couble, P., Germline transformation of the silkworm Bombyx mori L. using a piggyBac transposon-derived vector. Nat. Biotechnol., 18, 81–84 (2000).
  • 8) Thomas, J. L., Da Rocha, M., Besse, A., Mauchamp, B., and Chavancy, G., 3xP3-EGFP marker facilitates screening for transgenic silkworm Bombyx mori L. from the embryonic stage onwards. Insect Biochem. Mol. Biol., 32, 247–253 (2002).
  • 9) Imamura, M., Nakai, J., Inoue, S., Quan, G. X., Kanda, T., and Tamura, T., Targeted gene expression using the GAL4/UAS system in the silkworm Bombyx mori. Genetics, 165, 1329–1340 (2003).
  • 10) Suzuki, M. G., Funaguma, S., Kanda, T., Tamura, T., and Shimada, T., Role of the male BmDSX protein in the sexual differentiation of Bombyx mori. Evol. Dev., 7, 58–68 (2005).
  • 11) Uhlirova, M., Asahina, M., Riddiford, L. M., and Jindra, M., Heat-inducible transgenic expression in the silkmoth Bombyx mori. Dev. Genes Evol., 212, 145–151 (2002).
  • 12) Adachi, T., Tomita, M., Shimizu, K., Ogawa, S., and Yoshizato, K., Generation of hybrid transgenic silkworms that express Bombyx mori prolyl-hydroxylase alpha-subunits and human collagens in posterior silk glands: production of cocoons that contained collagens with hydroxylated proline residues. J. Biotechnol., 126, 205–219 (2006).
  • 13) Royer, C., Jalabert, A., Da Rocha, M., Grenier, A. M., Mauchamp, B., Couble, P., and Chavancy, G., Biosynthesis and cocoon-export of a recombinant globular protein in transgenic silkworms. Transgenic Res., 14, 463–472 (2005).
  • 14) Tomita, M., Munetsuna, H., Sato, T., Adachi, T., Hino, R., Hayashi, M., Shimizu, K., Nakamura, N., Tamura, T., and Yoshizato, K., Transgenic silkworms produce recombinant human type III procollagen in cocoons. Nat. Biotechnol., 21, 52–56 (2003).
  • 15) Inoue, S., Kanda, T., Imamura, M., Quan, G. X., Kojima, K., Tanaka, H., Tomita, M., Hino, R., Yoshizato, K., Mizuno, S., and Tamura, T., A fibroin secretion-deficient silkworm mutant, Nd-sD, provides an efficient system for producing recombinant proteins. Insect Biochem. Mol. Biol., 35, 51–59 (2005).
  • 16) Uchino, K., Imamura, M., Shimizu, K., Kanda, T., and Tamura, T., Germ line transformation of the silkworm, Bombyx mori, using the transposable element Minos. Mol. Genet. Genomics, 277, 213–220 (2007).
  • 17) Mita, K., Kasahara, M., Sasaki, S., Nagayasu, Y., Yamada, T., Kanamori, H., Namiki, N., Kitagawa, M., Yamashita, H., Yasukochi, Y., Kadono-Okuda, K., Yamamoto, K., Ajimura, M., Ravikumar, G., Shimomura, M., Nagamura, Y., Shin, I. T., Abe, H., Shimada, T., Morishita, S., and Sasaki, T., The genome sequence of silkworm, Bombyx mori. DNA Res., 11, 27–35 (2004).
  • 18) Takei, F., Oyama, F., Kimura, K., Hyodo, A., Mizuno, S., and Shimura, K., Reduced level of secretion and absence of subunit combination for the fibroin synthesized by a mutant silkworm, Nd(2). J. Cell Biol., 99, 2005–2010 (1984).
  • 19) Bendtsen, J. D., Nielsen, H., von Heijne, G., and Brunak, S., Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol., 340, 783–795 (2004).
  • 20) Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G., Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng., 10, 1–6 (1997).
  • 21) Waga, S., and Mizuno, S., Different behavior of chromatin domains encompassing fibroin heavy-chain gene in active, temporarily inactive, and permanently inactive transcriptional states in silk gland nuclei. J. Biol. Chem., 268, 6429–6436 (1993).
  • 22) Takiya, S., Hui, C. C., and Suzuki, Y., A contribution of the core-promoter and its surrounding regions to the preferential transcription of the fibroin gene in posterior silk gland extracts. EMBO J., 9, 489–496 (1990).
  • 23) Takei, F., Kikuchi, Y., Kikuchi, A., Mizuno, S., and Shimura, K., Further evidence for importance of the subunit combination of silk fibroin in its efficient secretion from the posterior silk gland cells. J. Cell Biol., 105, 175–180 (1987).
  • 24) Mori, K., Tanaka, K., Kikuchi, Y., Waga, M., Waga, S., and Mizuno, S., Production of a chimeric fibroin light-chain polypeptide in a fibroin secretion-deficient naked pupa mutant of the silkworm Bombyx mori. J. Mol. Biol., 251, 217–228 (1995).
  • 25) Du, X., and Thiem, S. M., Responses of insect cells to baculovirus infection: protein synthesis shutdown and apoptosis. J. Virol., 71, 7866–7872 (1997).
  • 26) Takano, E., Maki, M., Mori, H., Hatanaka, M., Marti, T., Titani, K., Kannagi, R., Ooi, T., and Murachi, T., Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis. Biochemistry, 27, 1964–1972 (1988).
  • 27) Tanaka, K., Inoue, S., and Mizuno, S., Hydrophobic interaction of P25, containing Asn-linked oligosaccharide chains, with the H-L complex of silk fibroin produced by Bombyx mori. Insect Biochem. Mol. Biol., 29, 269–276 (1999).
  • 28) Michal, C. A., Simmons, A. H., Chew, B. G., Zax, D. B., and Jelinski, L. W., Presence of phosphorus in Nephila clavipes dragline silk. Biophys. J., 70, 489–493 (1996).
  • 29) Zhang, P., Aso, Y., Yamamoto, K., Banno, Y., Wang, Y., Tsuchida, K., Kawaguchi, Y., and Fujii, H., Proteome analysis of silk gland proteins from the silkworm, Bombyx mori. Proteomics, 6, 2586–2599 (2006).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.