Bacterial single-stranded DNA-binding proteins (SSBs) recruit a diverse array of genome maintenance enzymes to their sites of action through direct protein interactions. The essential nature of these SSB-protein interactions makes inhibitors that block SSB-partner complex formation valuable biochemical tools and attractive potential antibacterial agents. However, many of these protein-protein interactions are weak and not amenable to the high-throughput nature of small molecule screens. Here I describe a high-throughput screen to identify small molecules that inhibit the interaction between Exonuclease I (ExoI) and the final 10 amino acids of the SSB C-terminal tail (SSB-Ct). The strength of the binding between ExoI and the SSB-Ct tail is fundamental to the interaction's utility in the high-throughput screen.
CITATION STYLE
Bernstein, D. A. (2012). Identification of Small Molecules That Disrupt SSB–Protein Interactions Using a High-Throughput Screen (pp. 183–191). https://doi.org/10.1007/978-1-62703-032-8_14
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