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SSB: Organizational center and Achilles heel

The C‐terminus (Ct) of the single‐strand DNA binding protein (SSB) from Escherichia coli forms a conserved binding site for numerous proteins involved in DNA replication, recombination, and repair. SSB stimulates the enzymatic activities of several of its partner proteins, notably Exonuclease I and RecQ helicase. This stimulation is thought to be a result of the physical interaction between the proteins, which is mediated by the SSB‐Ct. We have utilized NMR and X‐ray crystallography to map the sites of interaction for the SSB‐Ct in RecQ and Exonuclease I, respectively. Mutation of SSB‐Ct binding site residues in either protein results in loss of stimulation and/or inhibition by SSB. In addition to these biochemical studies, we have identified small molecule compounds that disrupt SSB interaction with Exonuclease I. With the essential nature of SSB protein interactions in bacteria, we hypothesized that these molecules could provide novel lead antibacterial compounds. Consistent with this hypothesis, the compounds are potent anti‐bacterial agents with little or no activity against eukaryotic cells.