PMC:1140370 / 17348-19199 JSONTXT

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Mcm4/6/7 bound to A-fork[3′,5′] with much lower affinity, and the complex gave rise to a single band. These findings indicate that the Mcm4/6/7 complex is loaded onto DNA preferentially and efficiently through single-stranded region, regardless of the presence of 3′- or 5′-terminus.\nIn contrast, only the substrate containing a 3′ single-stranded DNA tail (A-fork[5′]) was efficiently unwound and A-fork[3′] or A-fork[3′,5′], was not unwound by Mcm4/6/7 (Figure 4B). Absence of helicase actions on A-fork[3′,5′] composed only of duplex regions is expected since double-stranded DNA is not able to activate the ATPase activity of Mcm4/6/7 (10). In contrast, the PriA, a structure-specific helicase used as a control, binds at the fork junction and unwinds the fork and the nascent lagging strand DNA on A-fork[5′], or unwinds the nascent lagging strand on A-fork[3′,5′], as reported before (25). 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