Expression of Soluble Active Interferon αA in Escherichia coli Periplasm by Fusion with Thermostable Lichenase Using the Domain Insertion Approach

A recombinant DNA in which the interferon αA (IFN–αA) gene sequence is integrated into a loop region of the gene coding thermostable lichenase was constructed. This approach of insertion fusion with thermostable lichenase is advantageous in terms of increasing the solubility, stability, and producti...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2018-03, Vol.83 (3), p.259-269
Main Authors: Tyurin, A. A., Kabardaeva, K. V., Mustafaev, O. N., Pavlenko, O. S., Sadovskaya, N. S., Fadeev, V. S., Zvonova, E. A., Goldenkova-Pavlova, I. V.
Format: Article
Language:English
Subjects:
Bacteria
Biochemistry
Biological activity
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Deoxyribonucleic acid
DNA
E coli
Escherichia coli
Insertion
Interferon
Life Sciences
Microbiology
Nucleotide sequence
Periplasm
Recombinant DNA
Thermal stability
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Summary:A recombinant DNA in which the interferon αA (IFN–αA) gene sequence is integrated into a loop region of the gene coding thermostable lichenase was constructed. This approach of insertion fusion with thermostable lichenase is advantageous in terms of increasing the solubility, stability, and production of the fusion partner in soluble form in general and in the periplasm of bacterial cells in particular. Thus, the insertion of IFN–αA into the loop (53 a.a.) of thermostable lichenase from Clostridium thermocellum resulted in effective expression of the soluble form of the recombinant protein in the periplasm of Escherichia coli without any compromise in biological activity of IFN–αA, while the thermostable lichenase retained its ability for functional folding without dramatic loss of its basic activity and thermostability.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297918030069