Intein-Mediated Protein trans-Splicing of the Recombinant Streptavidin on Magnetosomes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2021-09-08

AUTHORS

S. B. Duan, S. S. Wei, H. M. Wang, S. H. Ding, Y. Z. Chen, J. J. Tian, Y. J. Wang, W. Chen, J. Chen, Q. L. Meng

ABSTRACT

When expressing streptavidin recombinant polypeptide on magnetosomes (called bacterial magnetic nanoparticles, or BMPs), the presence of endogenous bacterial biotin might be detrimental. In the study, the streptavidin monomer fragment (SA1–116) was fused with the intein N-terminal (termed precursor SA1–116-IN), and SA1–116-IN was expressed in E. coli (BL21). Meanwhile, the SA117–160 fragment was fused with the C-terminal intein, and then this chimeric polypeptide was expressed on magnetosomes by fusion with magnetosome membrance protein MamF. In the in vitro protein splicing system, the purified engineered magnetosomes (BMP-SA117–160-IC) and the SA1–116-IN precursor were mixed. Intein-mediated trans-splicing reaction was induced to produce the functional magnetic beads BMP-SA. Our results indicate that intein-mediated protein trans-splicing may lead to efficient synthesis of the recombinant streptavidin on the magnetosomes, showing its promising potential to produce other functional magnetic nanoparticles. More... »

PAGES

884-888

Identifiers

URI

http://scigraph.springernature.com/pub.10.1134/s0026893321050058

DOI

http://dx.doi.org/10.1134/s0026893321050058

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1141009055


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