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Bioscience, Biotechnology, and Biochemistry Volume 72, 2008 - Issue 8
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Original Articles

Construction of an Expression System for Aqualysin I in Escherichia coli That Gives a Markedly Improved Yield of the Enzyme Protein

Masayoshi SAKAGUCHIDepartment of Applied Chemistry, Kogakuin University
,
Keisuke NIIMIYADepartment of Applied Chemistry, Kogakuin University
,
Makoto TAKEZAWADepartment of Applied Chemistry, Kogakuin University
,
Tsutomu TOKIDepartment of Applied Chemistry, Kogakuin University
,
Yasusato SUGAHARADepartment of Applied Chemistry, Kogakuin University
&
Masao KAWAKITADepartment of Applied Chemistry, Kogakuin University
Pages 2012-2018 | Received 03 Mar 2008, Accepted 03 May 2008, Published online: 22 May 2014

  • 1) Matsuzawa, H., Hamaoki, M., and Ohta, T., Production of thermophilic extracellular proteases (aqualysin I and II) by Thermus aquaticus YT-1, an extreme thermophile. Agric. Biol. Chem., 47, 25–28 (1983).
  • 2) Matsuzawa, H., Tokugawa, K., Hamaoki, M., Mizoguchi, M., Taguchi, H., Terada, I., Kwon, S. T., and Ohta, T., Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1. Eur. J. Biochem., 171, 441–447 (1988).
  • 3) Siezen, R. J., and Leunissen, J. A., Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci., 6, 501–523 (1997).
  • 4) Kwon, S. T., Terada, I., Matsuzawa, H., and Ohta, T., Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteristics of the deduced primary structure of the enzyme. Eur. J. Biochem., 173, 491–497 (1988).
  • 5) Terada, I., Kwon, S. T., Miyata, Y., Matsuzawa, H., and Ohta, T., Unique precursor structure of an extracellular protease, aqualysin I, with NH2- and COOH-terminal pro-sequences and its processing in Escherichia coli. J. Biol. Chem., 265, 6576–6581 (1990).
  • 6) Lee, Y. C., Ohta, T., and Matsuzawa, H., A non-covalent NH2-terminal pro-region aids the production of active aqualysin I (a thermophilic protease) without the COOH-terminal pro-sequence in Escherichia coli. FEMS Microbiol. Lett., 71, 73–77 (1992).
  • 7) Sambrook, J., and Russell, D. W., “Molecular Cloning, a Laboratory Manual” 3rd edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor (2001).
  • 8) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).
  • 9) Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248–254 (1976).
  • 10) Louis, J. M., McDonald, R. A., Nashed, N. T., Wondrak, E. M., Jerina, D. M., Oroszlan, S., and Mora, P. T., Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli. Eur. J. Biochem., 199, 361–369 (1991).
  • 11) Wan, M., Takagi, M., Loh, B. N., Xu, X. Z., and Imanaka, T., Autoprocessing: an essential step for the activation of HIV-1 protease. Biochem. J., 316, 569–573 (1996).
  • 12) Kim, J. Y., Choi, Y. L., Cho, Y. S., Kim, C. H., and Lee, Y. C., Independently expressed N-terminal pro-domain of aqualysin I precursor complements the folding of its mature domain to active form in Escherichia coli. J. Basic Microbiol., 42, 181–189 (2002).
  • 13) Lee, Y. C., Miyata, Y., Terada, I., Ohta, T., and Matsuzawa, H., Involvement of NH2-terminal pro-sequence in the production of active aqualysin I (a thermophilic serine protease) in Escherichia coli. Agric. Biol. Chem., 55, 3027–3032 (1991).

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