Current Research

Biochemical and structural analysis of the E. coli replication restart proteins PriB and DnaT

All organisms encounter obstacles when replicating DNA. These obstacles take the form of DNA
damage, frozen protein-DNA complexes, or other irregularities in the DNA template and can cause the replisome to halt and dissociate completely. My research focuses on the replication restart pathways that E. coli and other bacteria have evolved to initiate origin-independent DNA replication at sites where a replisome has dissociated. Replisome dissociation leaves a DNA-fork structure that is problematic for the cell if not resolved. The replication restart proteins have evolved to bind these forks with high affinity and specificity, remodel the fork, and reload the replicative proteins back on the template DNA. My research is focused on understanding the biochemical and structural mechanisms by which this essential pathway operates.