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Displaying non-natural, functional molecules on yeast surfaces via biotin-streptavidin interaction
- Tanaka, Tsutomu, Masunari, Shinsuke, Ishii, Jun, Wakamura, Kanako, Segawa, Maiko, Fukuda, Hideki, Kondo, Akihiko
- Journal of biotechnology 2010 v.145 no.1 pp. 79-83
- Escherichia coli, biotechnology, biotin, streptavidin, yeasts
- 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.