A Novel Bacterial Approach for Detecting Protein-Protein Interactions Based on the Twin-Arginine Translocon
Eva-Maria Strauch, Department of Chemistry and Biochemistry, University of Texas at Austin, 2500 Speedway, Austin, TX 78712 and George Georgiou, Chemical Engineering, University of Texas at Austin, 1 University Station C0400, Austin, TX 78712

The detection of protein:protein interactions by in-vivo techniques such as yeast display and protein complementation assays has been instrumental in identifying drug targets and for the construction of biological networks. We have developed a bacterial system for the detection of protein:protein interactions that capitalizes on the remarkable properties of the bacterial Twin Arginine Transporter (Tat) pathway. This export pathway possesses the ability to export folded proteins, particularly those which need to fold prior to their export due to co-factor insertion, subunit assembly or those that fold too quickly for Sec export. The technology we have developed utilizes either growth on selective media or colorimetric detection of interacting protein pairs. Furthermore, it can be used as a platform to increase protein-protein affinity or to increase solubility.

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