Zoe Wetmore

Elucidating the Mechanism of RecOR Mediated RecA Loading in E. coli ssDNA Gap Repair

Homologous recombinational repair of DNA is critical for maintaining genomic integrity and is used in resolving postreplication single strand (ss) DNA gaps that can arise in response to DNA damage. In E. coli, the gap repair process is dependent on the protein RecA, which recruits homologous template DNA that can be used by the repair machinery to fix the ssDNA gap. RecA must bind the ssDNA gap in order to perform its repair functions, but binding is often blocked by single strand DNA binding protein (SSB), which functions to protect the ssDNA gap from further damage but must ultimately be removed for homologous repair of the gap to occur. The RecOR protein complex is known to enhance RecA loading on SSB coated ssDNA, but the details of how it does so remain poorly understood. My research focuses on deepening our mechanistic understanding of how E. coli RecOR removes SSB from ssDNA gaps so RecA can be loaded using biochemical, structural, and genetics approaches.