Expression of a recombinant molt-inhibiting hormone of the kuruma prawn penaeus japonicus in escherichi coli

Bioscience, Biotechnology and Biochemistry

Volumn 63, Issue 9, 1999, Pages 1576-1581

  Ohira, Tsuyoshi ^a   Nishimura, Takayuki ^b   Sonobe, Haruyuki ^b   Okuno, Atsuro ^a   Watanabe, Toshiki ^c   Nagasawa, Hiromichi ^a   Kawazoe, Ichiro ^a   Aida, Katsumi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b KONAN UNIVERSITY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

Bacterial expression; Crustacean; Molt inhibiting hormone; Molting; Penaeus japonicus

Indexed keywords

HORMONE; MOLT INHIBITING HORMONE; MOLT-INHIBITING HORMONE; PRIMER DNA; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMISTRY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; GROWTH, DEVELOPMENT AND AGING; NUCLEOTIDE SEQUENCE; PENAEIDAE; PHYSIOLOGY; PLASMID; PROTEIN FOLDING;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; DNA PRIMERS; ESCHERICHIA COLI; GENE EXPRESSION; INVERTEBRATE HORMONES; PENAEIDAE; PLASMIDS; PROTEIN FOLDING; RECOMBINANT PROTEINS;

EID: 0033195419     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1576     Document Type: Article

References (20)

1. Keller, R., Crustacean neuropeptides: structures, functions and comparative aspects. Experientia, 48, 439-448 (1992).
2. Chang, E. S., Prestwich, G. D., and Bruce, M. J., Amino acid sequence of a peptide with both molt-inhibiting and hyperglycemic activities in the lobster, Homarus americanus. Biochem. Biophys. Res. Commun., 171, 818-826 (1990).
3. Webster, S. G., Amino acid sequence of putative molt-inhibiting hormone from the crab, Carcinus maenas. Proc. R. Soc. Lond. B, 244, 247-252 (1991).
4. Yang, W. J., Aida, K., Terauchi, A., Sonobe, H., and Nagasawa, H., Amino acid sequence of a peptide with molt-inhibiting activity from the kuruma prawn Penaeus japonicus. Peptides, 17, 197-202 (1996).
5. Aguilar, M. B., Falchetto, R., Shabanowitz, J., Hunt, D. F., and Huberman, A., Complete primary structure of the molt-inhibiting hormone (MIH) of the mexican crayfish Procambarus bouvieri (Ortmann). Peptides, 17, 367-374 (1996).
6. Nagasawa, H., Yang, W. J., Shimizu, H., Aida, K., Tsutsumi, H., Terauchi, A., and Sonobe, H., Isolation and amino acid sequence of a molt-inhibiting hormone from the American crayfish, Procambarusclarkii. Biosci. Biotechnol. Biochem., 60, 554-556 (1996).
7. Lachaise, F., Le Roux, A., Hubert, M., and Lafont, R., The molting gland of crustaceans: localization, activity, and endocrine control. J. Crustacean Biol., 13, 198-234 (1993).
8. Webster, S. G. and Keller, R., Purification, characterization and amino acid composition of the putative moult-inhibiting hormone (MIH) of Carcinus maenas (Crustacea, Decapoda). J. Comp. Physiol., 156, 617-624 (1986).
9. Terauchi, A., Tsutsumi, H., Yang, W. J., Aida, K., Nagasawa, H., and Sonobe, H., A novel neuropeptide with molt-inhibiting activity from the sinus gland of the crayfish, Procambarus clarkii. Zool. Sei., 13, 295-298 (1996).
10. Ohira, T., Watanabe, T., Nagasawa, H., and Aida, K., Molecular cloning of a molt-inhibiting hormone cDNA from the kuruma prawn Penaeus japonicus. Zool. Sei., 14, 785-789 (1997).
11. Yin, H. L-, Iida, K., and Janmey, P. A., Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments. J. Cell Biol., 106, 805-812 (1988).
12. Sonobe, H., Kamba, M., Ohta, K., Ikeda, M., and Naya, Y., In vitro secretion of eedysteroids by Y-organs of the crayfish, Procambarus clarkii. Experientia, 47, 948-952 (1991).
13. Langley, K. E., Berg, T. F., Strickland, T. W., Fenton, D. M., Boone, T. C., and Wypych, J., Recombinant-DNA-derived bovine growth hormone from Escherichia coli. 1. Demonstration that the hormone is expressed in reduced form, and isolation of the hormone in oxidized, native form. Eur. J. Biochem., 163, 313-321 (1987).
14. Sato, N., Kawazoe, I., Tamai, T., Inoue, Y., Murata, K., Kimura, S., Nonaka, M., and Kimura, A., Purification and characterization of recombinant tuna growth hormone produced in Escherichia coli. J. Ferment. Bioeng., 68, 79-83 (1989)
15. Trant, J. M., Heterologous expression of the spiny dogfish shark (Squalus acanthias) cytochrome P450cl7 (173-hydroxylase) in Escherichia coli. Gen. Comp. Endcrinol., 102, 173-182 (1996).
16. Ben-Bassat, A. and Bauer, K., Amino-terminal processing of proteins. Nature, 326, 315 (1987).
17. Ben-Bassat, A., Bauer, K., Chang, S. Y., Myambo, K., Boosman, A., and Chang, S., Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine amino-peptidase and its gene structure. J. Bacteriol., 169, 751-757 (1987).
18. Han, B., Hall, F. L., and Nimni, M. E., Refolding of a recombinant collagen-targeted TGF-β2 fusion protein expressed in Escherichia coli. Protein Expr. Purif., 11, 169-178 (1997).
19. Cardamone, M., Puri, N. K., and Brandon, M. R., Comparing the refolding and reoxidation of recombinant porcine growth hormone from a urea denatured state and from Escherichia coli inclusion bodies. Biochemistry, 34, 5773-5794 (1995).
20. Gasparini, S., Kiyatkin, N., Drevet, P., Boulain, J. C., Tacnet, F., Ripoche, P., Forest, E., Grishin, E., and Menez, A., The low molecular weight protein which co-purifies with d-latrotoxin is structurally related to crustacean hyperglycemichormones. J. Biol. Chem., 269, 19803-19809 (1994).