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Displaying non-natural, functional molecules on yeast surfaces via biotin–streptavidin interaction

Paper ID Volume ID Publish Year Pages File Format Full-Text
24577 43527 2010 5 PDF Available
Title
Displaying non-natural, functional molecules on yeast surfaces via biotin–streptavidin interaction
Abstract

Here we expand the yeast cell surface display system to display non-natural, functional molecules. The short biotin acceptor peptide (BAP) sequence of biotin ligase from E. coli (BirA) was genetically introduced to the N-terminus of the anchor protein, Flo428. Through co-expression of BAP-fused Flo428 with BirA, biotinylated BAP could be displayed on the yeast cell surface. Subsequent addition of streptavidin–FITC resulted in the display of streptavidin–FITC, and, the display of biotin–FITC was successful using streptavidin as a linker. Our strategy provides a powerful tool for displaying functional molecules on yeast cell surfaces.

Keywords
BAP, biotin acceptor peptide; BirA, biotin ligase from E. coli; FITC, fluorescein isothiocyanate; FACS, flow cytometric cell soortingCell surface display; Yeast; Biotin; Streptavidin; Biotin ligase
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Displaying non-natural, functional molecules on yeast surfaces via biotin–streptavidin interaction
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 145, Issue 1, 1 January 2010, Pages 79–83
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us