B.S. (1995): Peking University, Beijing, China
M.S. (1997): Rutgers University at New Brunswick
Ph.D. (2003): University of California at Berkeley
Postdoctoral Associate (2003-2006): Harvard Medical School
Assistant Professor (2006-2013): University of Chicago
Associate professor (2013-present): Georgia State University
Chemical Biology, Bioorganic Chemistry
The cell is operating on multilayers of complexities to sustain its life cycle. The regulatory networks in the cell is complex in that the activities of cellular proteins are switched on and off by many types of posttranslational modifications such as phosphorylation, glycosylation and ubiquitination. The chemical transformations in the cell are also complex for the assembly of natural products of diverse structures through a myriad of biosynthetic pathways. The branch of chemical biology based on synthetic small molecules has provided inhibitors, activity-based probes, and imaging reagents to study cellular processes. However the complexities of the cell are far beyond the capacity of using small molecules to probe the biological mechanisms. We are thus developing another branch of chemical biology based on the “synthetic proteins” – engineered proteins with desired catalytic or binding properties, to investigate and manipulate the cellular processes. We have so far engineered the ubiquitin (UB) transfer cascade to map and reprogram signaling pathways mediated by protein ubiquitination. We have also engineered the natural product biosynthetic enzymes to harness the chemical transformations in the cell for the synthesis of drug molecules.
Engineering an orthogonal ubiquitin transfer cascade
- Zhao, B., Bhuripanyo, K., Zhang, K., Kiyokawa, H., Schindelin, H. & Yin, J. (2012). Orthogonal Ubiquitin Transfer through Engineered E1-E2 Cascade for Protein Ubiquitination. Chem Biol, 19, 1265-77.
- Zhang, K., Nelson, K. M., Bhuripanyo, K., Grimes, K. D., Zhao, B., Aldrich, C. C. & Yin, J. (2013). Engineering the substrate specificity of the DhbE adenylation domain by yeast cell surface display. Chem Biol, 20, 92-101.
- Zhao, B., Bhuripanyo, K., Schneider, J., Zhang, K., Schindelin, H., Boone, D. & Yin, J. (2012). Specificity of the E1-E2-E3 Enzymatic Cascade for Ubiquitin C-terminal Sequences Identified by Phage Display. ACS Chem Biol, 7, 2027-35.
- Zhang, K., Lin, H., Bhuripanyo, K., Zhao, B., Zheng, N., and Yin, J. (2013) Engineering New Protein-Protein Interactions on the β-Propeller Fold by Yeast Cell Surface Display, ChemBioChem 14, 426-30.
- Zhao, B., Zhang, K., Villhauer, E. B., Bhuripanyo, K., Kiyokawa, H., Schindelin, H., and Yin, J. (2013) Phage display to identify nedd8-mimicking peptides as inhibitors of the nedd8 transfer cascade, Chembiochem 14, 1323-1330.