Our research is focused on the molecular mechanism of genetic recombination. Our laboratory is examining this process by characterizing the proteins that are essential to genetic recombination in Prokarya, Eukarya, and Archaea. The goal of our work is to establish an in vitro system that accurately reproduces the cellular process. In all organisms, the first step of recombination is the processing of this dsDNA interruption into a substrate suitable for the action of a DNA pairing protein.
Processing is mediated by the combined action of a helicase and nuclease.
Finally, the homologously paired DNA intermediates are resolved. In E. coli, RecA protein promotes a reaction that is both biochemically unique and central to the recombination process, namely, the homologous pairing and exchange of DNA strands. The RecBCD enzyme unwinding, and degrades, the DNA until recognition of the cis-acting DNA regulatory sequences known as Chi. Finally, the RecO and RecR proteins contribute to the recombination process by mediating the exchange of ssDNA-bound SSB protein for RecA protein. In S. cerevisiae, Rad51 protein is a homolog of the RecA protein, and RPA protein is the homologue of the SSB protein.