Abstract
Effective DNA replication and repair is crucial to the survival of all organisms and necessitates the cooperation of a variety of macromolecules. In Escherichia coli, the DNA Polymerase III holoenzyme is one of these macromolecules which, along with being the main contributor to DNA replication, is known to participate in other interactions which aid in the repair of damaged DNA. One such interaction is with YoaA, a putative helicase found to promote tolerance to replication inhibiting factors. The interaction between YoaA and the DNA Polymerase III holoenzyme takes place at HolC, one of the holoenzyme’s protein subunits. This project seeks to further characterize the interaction between YoaA and HolC while also attempting to identify the types of DNA damage and repair to which YoaA responds. Through Yeast Two-Hybrid, I have shown that the C-terminus of YoaA is the region responsible for HolC binding. Additionally, E. coli growth assays show that mutations in the C-terminus of YoaA may alter the protein’s function in vivo. A variety of phenotypic assays have suggested that YoaA does not exhibit a significant response to recombination events or point mutations.