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High-level expression of tamavidin 2 in human cells by codon-usage optimization.

Yoshimitsu Takakura1, Sakurako Katayama, Yuki Nagata

  • 1a Plant Innovation Center , Japan Tobacco Inc. , 700 Higashibara, Iwata, Shizuoka 438-0802 , Japan.

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PubMed
Summary

Tamavidin 2, a fungal protein, was engineered for high-level expression in human cells. This optimized protein maintains high biotin-binding affinity and thermal stability for mammalian cell applications.

Keywords:
biotincodon usageexpressionmammalian celltamavidin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Tamavidin 2 is a fungal protein with exceptional biotin-binding affinity and thermal stability, outperforming avidin and streptavidin.
  • Current limitations include poor expression in mammalian cells, hindering its use as an affinity tag in these systems.

Purpose of the Study:

  • To optimize codon usage of Tamavidin 2 for enhanced expression in human cells.
  • To enable the application of Tamavidin 2 as a robust affinity tag in mammalian cell systems.

Main Methods:

  • Codon optimization of the Tamavidin 2 gene for human codon usage.
  • Expression of the optimized Tamavidin 2 in human cells.
  • Purification using iminobiotin affinity chromatography.
  • Characterization of binding affinity and thermal stability.

Main Results:

  • The codon-optimized Tamavidin 2 mutant showed a 30-fold increase in expression levels in human cells compared to the native gene.
  • The purified protein exhibited high biotin-binding affinity and remained stable at 82°C.
  • Successful purification via iminobiotin affinity chromatography was achieved.

Conclusions:

  • High-level expression of Tamavidin 2 in mammalian cells is achievable through codon optimization.
  • This engineered Tamavidin 2 is a stable and high-affinity biotin-binding protein suitable for mammalian cell applications.
  • This technology facilitates the evaluation of fusion proteins in mammalian systems.