PMC:1140370 / 2198-3663 JSONTXT

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Consistent with this notion, the processivity of the Schizosaccharomyces pombe and mouse Mcm4/6/7 complexes is significantly stimulated on forked DNA structures and it can unwind duplex DNA of 400–500 bp (13,14). Mcm4/6/7 binds to fork and bubble structures in an ATP-dependent manner, and generates a double-hexameric complex, as was shown for T-antigen (13,14,21). Recently, we reported that the helicase and ATP hydrolysis activities of mammalian Mcm4/6/7 are specifically activated by single-stranded DNA containing stretches of thymine residues and proposed a novel model that Mcm may play a crucial role in selection of replication origins in higher eukaryotes 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