Team:Berkeley/Project/Zippers

Protein interaction domain-peptide systems have been used by synthetic biologists to oligomerize or localize proteins. In particular, protein-protein interaction pairs have been applied to both scaffolding and signaling applications with impressive results. In such systems, orthogonality of protein pair interactions is desired to reduce cross-talk between system components and allow synthetic biologists to gain more precise control over a system. However, the limited number and diversity of well-characterized, orthogonal protein interaction domains restricts the complexity of systems that can be designed.

Current screening methods for protein-protein interactions (such as transcription-driven GFP expression in yeast 2-hybrid systems) do not have high enough throughput to analyze large library sizes of protein interaction pairs. However, with the utilization of MiCodes and microscopy’s ability to record spatial information, we were able to design an assay to directly observe and screen for orthogonal protein-protein interactions.