Abstract

The small subunit of the bacteriophage λ terminase enzyme, the product of the phage's Nu1 gene, is shown to contain amino acid segments homologous to those present in a large number of ATPases. In keeping with these predictions, the purified protein has been found to hydrolyze ATP with a relatively low turnover number. Terminase holoenzyme is a known ATPase, and the biochemical significance of an ATP-interactive center situated in the gpNu1 subunit is discussed.

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