Training. The primary emphasis of our lab is to teach students (starting as early as possible in their career) how to approach scientific problems, and then how to design and execute rigorous and relevant experiments to address these problems. Our published papers contribute to the understanding of how E. coli does what it does.
An electron micrograph of E. coli - our model organism (Thanks Vik!)
Bacterial two-hybrid assay (B2H). Protein/protein interactions underpin how E. coli does what it does. We utilize the B2H assay that was developed in Ann Hochschild’s Lab at Harvard Medical School to uncover and dissect these interactions. Lower left: Agar plate of ‘bioart’ prepared with our new B2H strain that harbored either interacting or non-interacting protein/protein pairs and imaged under regular light. Lower right: sample plate visualized for fluorescence.
Genetics. Crystal structure (PMID: 12016306) and my wooden interpretation(!) of a bacterial RNA polymerase (RNAP). A particular focus of the lab that is complementary to, and sometimes guided by crystallographic studies, is to dissect how transcription factors interact with RNAP to modulate its functional properties.
Coreome. To unmask protein binding determinants on RNA polymerase (RNAP) the RNAP core enzyme was parsed into 30+ discrete, surface exposed, independently folded fragments. Using this “coreome library” we can reveal protein binding sites on RNAP and subsequently dissect those interactions.
Tracking RNA polymerase. Using a variety of molecular biology and biochemical techniques we characterize RNAP activity both within E. coli cells and in highly purified in vitro systems.