Protein-protein interactions with the acidic COOH terminus of the single-stranded DNA-binding protein of the bacteriophage T4.

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Abstract
The single-stranded DNA-binding protein of the bacteriophage T4 is encoded by gene 32. Monoclonal antibodies were raised against intact gene 32 protein (gp32). We mapped the epitopes recognized by 12 of these monoclonal antibodies; the epitopes are all within the COOH-terminal region of gp32. As shown by others, removal of the COOH terminus of gp32 abolishes the ability of the intact protein to bind to many T4 proteins involved in replication, recombination, repair, and late transcription. These results suggest that the COOH terminus of gp32 is a protein-binding domain. The COOH terminus is attached to a DNA-binding domain that includes a zinc finger. We propose a model in which the DNA-binding and protein-binding domains are used in T4 replication, recombination, repair, and late transcription. The COOH terminus of gp32 is very acidic and may form four negatively charged amphipathic alpha-helices, which could fold into a four-helix bundle when associated with other proteins. At least six of the monoclonal anti-gp32 antibodies bind to the COOH terminus of gp32 and to DNA. Similarities between the COOH terminus of gp32 and DNA are explored.