№ 4 / 2016 / 32-38

Codon optimization of gene of tobacco etch virus protease for expression in E. COLI cells

Author: Ryabchenko A.V.¹, Kotova M.V.², Polyakov L.M.³

Abstract

The article presents data on codon optimization of gene of tobacco etch virus protease (TEVp) to increase the production of enzyme in E. coli cells. 37 synonymous mutations into rare codons and 4 mutations (T17S, N68D, I77V, S219V) were made in TEVp gene. The gene was cloned into the vector as the fused sequence with the gene of maltose-binding protein (MBP) and without it. The results of protein purification under native conditions from producer cells revealed that the greatest amount of enzyme was obtained with the construction of fusion genes MBP-TEVp.

Key words

tobacco etch virus protease, TEVp, recombinant protein, codon optimization, E. coli

References

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About Authors (Correspondence):

Ryabchenko A.V. – candidate of biological sciences, senior researcher of laboratory of medical biotechnology, e-mail: borrelia@mail.ru

Kotova M.V. – postgraduate student of laboratory of medical biotechnology, e-mail: zerokiri@mail.ru

Polyakov L.M. –doctor of medical sciences, professor, head of the laboratory of medical biotechnology, e-mail: plm@niibch.ru

Received: 31/08/2016