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. 2007 Apr 20;189(12):4502–4509. doi: 10.1128/JB.00376-07

FIG. 2.

FIG. 2.

(A) Purification and characterization of His-PcrAH− protein. (A) SDS-PAGE of purified His-PcrAH−. M, molecular weight markers; U and I, protein lysates from uninduced or isopropyl-β-d-thiogalactopyranoside-induced cells, respectively; P, 500 ng purified His-PcrAH− protein. (B) ATPase activity of PcrAH−. Various concentrations of wild-type (wt) PcrA or PcrAH− were tested for ATP hydrolysis in the presence or absence of ssDNA by TLC on polyethyleneimine-cellulose. (C) DNA binding activity of PcrAH−. DNA binding activities of wild-type PcrA and PcrAH− were analyzed by electrophoretic mobility shift assays using three different DNA probes. P, free probe; C, DNA-protein complex. (D) Helicase activities of PcrA and PcrAH− in the presence of a folded DNA substrate. ds, partially double-stranded probe; ss, single-stranded product; C, DNA-protein complex. (E) Helicase activities of PcrA and PcrAH− in the presence of partially duplex substrates containing either 3′ or 5′ ss dT tails. The structures of the various DNA substrates used are represented schematically at the bottom of the gel.