Abstract
The MCM helicase is an integral component of the DNA replication machinery. This ring‐shaped enzyme binds double‐stranded DNA (dsDNA) as an inactive double‐hexamer at replication origins. Once activated, the two single hexamers proceed to unwind duplex DNA by encircling single‐stranded DNA (ssDNA) during this movement. Previous studies of the N‐terminal domain of archaeal Pyrococcus furiosis MCM (PfMCM) showed ssDNA bound perpendicular to the central channel of the ring; defined as a conserved MCM ssDNA‐binding motif (MSSB). Using this same model we seek to determine the mode in which dsDNA is bound within the central channel of the ring prior to activation. Initial findings show PfMCM in its double hexamer form and it is anticipated that further examination with various dsDNA substrates will reveal by what means this helicase interacts with dsDNA upon loading. These studies aim to define fundamental aspects of the DNA replication processes.
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