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Method for protein overexpression

  • School of Agricultural Science/Graduate School of Bioagricultural Sciences
  • Laboratory of Molecular Biotechnology

Hideo Nakano [Professor]

http://www.agr.nagoya-u.ac.jp/~molbiote/index-e.html

  • School of Agricultural Science/Graduate School of Bioagricultural Sciences
  • Laboratory of Molecular Biotechnology

Teruyo Kato [Researcher]

Outline of Seeds

This technology makes it possible to easily increase the yield of the non-producible proteins for which heterologous expression is difficult.
We discovered that inserting twelve bases coated with four amino acids (SKIK) immediately after the initiating codon for the target gene resulted in a dramatic jump in yield for difficult-to-express proteins like E. coli and yeasts.

Novelty and originality of this research

・Because our method only involves inserting twelve bases immediately after the initiating codon for the target gene, it can be tested easily and in a short period of time.
・Effects have been seen in protein production in typical host microorganisms like E. coli and yeasts.

Application and research area for Industry collaboration

・Production of non-producible proteins (enzymes, antibodies, peptides, etc.)
・Application to hosts other than E. coli and yeasts
・Application to secretory proteins, membrane proteins, and the like
・Refining and detection tag applications

Key Takeaway

Our technology can be tested easily and at low cost.

Keywords

Non-producible proteins, E. coli, yeasts, high-yield protein production

Monographs, Papers and Articles

  • Ojima-Kato, T., Nagai, S. and Nakano,H. An N-terminal SKIK peptide tag markedly improves expression of difficult-to-express proteins in Escherichia coli and Saccharomyces cerevisiae. J. Biosci. Bioeng. 10.1016/j.jbiosc.2016.12.004 (2017) in press