The integrity of DNA is constantly challenged by exogenous and endogenous factors. Many proteins are involved in this constant battle to maintain genomic stability. The protein RecA is one of many proteins up regulated during the bacterial DNA damage response. It serves a variety functions one of which is Homologous Recombination at the site of double stranded DNA breaks. RecA preforms this function by forming nucleoprotein filaments on the single stranded regions of DNA, and mediating strand invasion of another homologous DNA molecule. After DNA pairing RecA gets off the DNA and DNA synthesis occurs. Our lab is interested in another DNA damage induced protein DinD that has been shown to inhibit RecA's activity. Previous work done in our lab has shown when added to a reaction where RecA is preforming DNA pairing DinD freezes the reaction. Inhibition of RecA's function could be attributed to sequestering DNA binding sites from the recombinase. However, further analysis also showed that DinD was not just sequestering binding sites on DNA, but instead it was disassembling the nucleoprotein filament of RecA. The in vivo functions of this activity are not completely understood. However, it is reasonable to think that under heavy DNA damage it is important for RecA to get off the DNA and allow faster synthesis. Here we present experiments designed to investigate whether DinD acts this way under DNA stress to allow for efficient DNA synthesis.