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ATPase activity of purified His-tagged PcrASpn. The dATPase activity of the pneumococcal helicase was measured by determining the hydrolysis of [α-32P]dATP. The reactions were performed in 1× TEKEM buffer containing 1 μCi of [α-32P]dATP and different amounts of His-PcrASpn. The ATPase activity of His-PcrASpn was activated by the presence of 100 ng of a 53-nt oligonucleotide (ssDNA). The products of [α-32P]dATP hydrolysis were analyzed by thin-layer chromatography.
