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pYD1 vector酵母表面展示载体
Introduction
pYD1 is a 5.0 kb expression vector designed for expression, secretion, and display of
proteins on the extracellular surface of Saccharomyces cerevisiae cells. Features of this
vector allow regulated expression, secretion, and detection of expressed proteins (see pages
15-16 for more information). The vector contains the following elements:
• AGA2 gene from Saccharomyces cerevisiae. This gene encodes one of the subunits of the
a-agglutinin receptor. Fusion of the gene of interest to AGA2 allows secretion and
display of the protein of interest.
• GAL1 promoter for regulated expression of the AGA2 gene fusion.
• Xpressô epitope and V5 epitope for detection of the displayed protein.
• Polyhistidine (6xHis) tag for detection and possible purification on metal chelating resin.
• TRP1 gene for selection in Saccharomyces cerevisiae.
• CEN6/ARS4 for stable, episomal replication in yeast.
• Ampicillin resistance gene and the pUC origin for selection and replication in E. coli.
Agglutinin
Receptor
The native a and α agglutinin receptors are believed to act as adhesion molecules to
stabilize cell-cell interactions during mating and to facilitate fusion between the a and
α haploid yeast cells. The Yeast Display System uses the a-agglutinin receptor of
S. cerevisiae to display foreign proteins on the cell surface (Boder and Wittrup, 1997).
The a-agglutinin receptor consists of two subunits encoded by the AGA1 and AGA2
genes (see diagram below). The Aga1 protein (Aga1p, 725 amino acids) is secreted
from the cell and becomes covalently attached to β-glucan in the extracellular matrix of
the yeast cell wall (Lu et al., 1995). The Aga2 protein (Aga2p, 69 amino acids) binds to
Aga1p through two disulfide bonds and after secretion remains attached to the cell
through its contact with Aga1p (Cappellaro et al., 1994; Cappellaro et al., 1991; Roy et
al., 1991). The N-terminal portion of Aga2p is required for attachment to Aga1p, while
proteins and peptides can be fused to the C-terminus for presentation on the yeast cell
surface (Boder and Wittrup, 1997).
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