Specific interactions between proteins form the basis of most biological processes, thus the knowledge of an organism’s protein interaction network provides insights into the function(s) of individual proteins, the structure of functional complexes, and eventually, the organization of the whole cell. The Protein-protein interactions (PPIs) can be detected by plenty of experimental methods. However, the yeast two-hybrid system (Y2H) is the most popular method to identify binary PPIs in vivo (Figure 1).
Figure 1 Yeast two-hybrid principle
A protein of interest ‘B’ is expressed in yeast as a fusion to a Gal4p DNA-binding domain (DBD, “bait”; circles denote expression plasmids). Another protein or library of proteins of interest ‘ORF’ is fused to Gal4p transcriptional activation domain (AD, “prey”). The two yeast strains are mated to combine the two plasmids expressing bait and prey fusion proteins in the same cell (diploid). If, proteins ‘B’ and ‘ORF’ interact in the resulting diploids cells, they reconstitute a transcription factor which activates a reporter gene (HIS3) and therefore allows the cell to grow on selective synthetic media (media lacking histidine).
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