Currently, little is understood about how archaeal replication proteins work together as a replisome complex for fast and efficient genome replication. We aim to understand the individual replisome components, including the Family B and D DNA polymerases, helicases and accessory proteins and how they work together to start replication, synthesize the chromosome and terminate. In addition, we are interested in discovering novel replication factors important for replication dynamics.
We aim to understand the molecular basis for DNA polymerase synthesis and fidelity. Pictured is a three-dimensional structural model of a DNA polymerase (from Andrew F. Gardner, Kiserian M. Jackson, Madeleine M. Boyle, Jackson A. Buss, Vladimir Potapov, Alexandra M. Gehring, Kelly M. Zatopek, Ivan R. Corrêa, Jr., Jennifer L. Ong, and William E. Jack (2019) Therminator DNA Polymerase: Modified Nucleotides and Unnatural Substrates. Front Mol Biosci. 6:28. doi: 10.3389/fmolb.2019.00028)