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Background  The hetero-hexamer of the eukaryotic minichromosome maintenance (MCM) proteins plays an essential role in replication of genomic DNA. The ring-shaped Mcm2-7 hexamers comprising one of each subunit show helicase activity  in vitro , and form double-hexamers on DNA. The Mcm4/6/7 also forms a hexameric complex with helicase activity  in vitro .    Results  We used an  Escherichiai coli  expression system to express various domains of  Schizosaccharomyces pombe  Mcm4, 6 and 7 in order to characterize their domain structure, oligomeric states, and possible inter-/intra-subunit interactions. We also successfully employed a co-expression system to express Mcm4/6/7 at the same time in  Escherichiai coli , and have purified functional Mcm4/6/7 complex in a hexameric state in high yield and purity, providing a means for generating large quantity of proteins for future structural and biochemical studies.    Conclusions  Based on our results and those of others, models were proposed for the subunit arrangement and architecture of both the Mcm4/6/7 hexamer and the Mcm2-7 double-hexamer.

Expression, purification and biochemical characterization of Schizosaccharomyces pombe Mcm4, 6 and 7