Presentation description

Protein tethering induces forcible dimerization of two proteins to solve mechanistic inquires. This phenomenon holds an array of uses in biochemistry, some of which include finding the interaction site of proteins, determining which proteins are necessary in a system, and confirming sites of protein localization. My project largely focuses on the differences and similarities between the PYL-ABI and FRB-FKBP protein tethering systems. The FRB-FKBP system can occasionally show drawbacks concerning an impact on the physiology of yeast cells. The alternative that I am exploring is the PYL-ABI system. This system uses Abscisic acid to dimerize and requires only two alleles, while the FRB-FKBP system uses Rapmycin and requires four alleles. The PYL-ABI system weeds out the issue of altered physiology with the added benefit of less time needed to show the same results. Although the PYL-ABI system can be easier, creating a strain with both systems can also be beneficial. Therefore, both systems have their own qualities and can be used interchangeably or simultaneously depending on the context.