Our goal is to understand the process of DNA transposition by crystallizing specific Hermes-DNA complexes at various stages of the transposition reaction. We hope that by understanding how the Hermes protein catalyzes DNA breakage and re-joining reactions, we will gain insights into its mechanism and regulation, allowing us to optimize Hermes (and perhaps other eukaryotic transposases) for use as a genetic tool in eukaryotic cells.
The basic research we are performing is aimed at understanding the various biochemical mechanisms by which discrete pieces of DNA move from one place in the genome to another. This process is called DNA transposition. In particular, we have been studying the eukaryotic transposon, Hermes, an active hAT transposon originally isolated from Musca domestica (the housefly). We have obtained the crystal structure of the protein alone, in complex with its transposon ends, and hope to extend this work to the characterization of other steps in the transposition reaction.