Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
24577 | Journal of Biotechnology | 2010 | 5 Pages |
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.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Tsutomu Tanaka, Shinsuke Masunari, Jun Ishii, Kanako Wakamura, Maiko Segawa, Hideki Fukuda, Akihiko Kondo,