Innovative, highly-efficient strategies to purify proteins of interest, determine their genomic binding sites, and target their activity to desired genomic regions

Description:

Title: A Unified Strategy to Simplify and Enhance Studies of Protein Function

Protein studies are universal across disciplines in biological sciences. Because of this ubiquity, numerous strategies exist to purify, localize, redirect, deplete, and visualize proteins in all model organisms. However, it can be cumbersome to create required strains to investigate the many different aspects of protein function. Even in yeast, one of the “simplest” model organisms, there is no streamlined approach that allows for robust protein localization and purification from a single strain. Instead, there are a host of unique N- and C-terminal tags that can be added for different desired applications.

Disclosed herein is a unified approach that can be used to assess many aspects of protein function, providing advantages such as speed, simplicity, and efficiency across multiple fields.  ­The three specific goals herein are to create a robust, highly-efficient strategy to rapidly purify proteins from source, to develop a new, antibody- free method for high-resolution mapping of protein-DNA binding sites across the genome, and to design a method to localize proteins of interest to desired chromatin locations. All of these strategies employ application of the SpyCatcher-SpyTag system in an innovative and modular way.  More broadly, this research lays the foundation to alter the way researchers work with particular proteins. Instead of requiring disparate tagging strategies to dissect different aspects of protein function, we are highlighting the ability to use a single tagging strategy with well-defined, modular adapters to easily investigate multiple aspects of protein function.

Patent 11,236,326

Patent Information:
For Information, Contact:
Christine Gramer
Senior Technology Development Associate
University of Oregon
cgramer@uoregon.edu
Inventors:
Jeff McKnight
Keywords:
Science