The MCM-binding protein (MCMBP) promotes the hexamer assembly of the replicative MCM2–7 helicase by interacting with the nascent MCM3 subunit, playing a key role in achieving high expression levels of the functional MCM2–7 helicase for maintaining genome integrity.

The crystal structure of the MCM helicase bound to single-stranded DNA reveals a binding motif that is critical for cell viability, helicase activation and DNA replication.

The hexametric structures of MCM8/9, revealed through cryo-electron microscopy single particle analysis, provide a foundational understanding of its helicase activity and offer novel insights into its mechanistic role.

Replication origins are established throughout the genome with the exception of transcribed genes, and the local chromatin composition likely modulates the density of ORC and MCM as well as origin activation.

The Mcm2-7 motor unwinds DNA using an approach distinct from that of superfamily III helicases, and accesses multiple ring configurations and assembly states during the initiation of DNA replication.

Mcm2 promotes mouse embryonic stem cells differentiation through manipulating chromatin landscapes at bivalent chromatin domains.

Building on previous work (Froelich et al., 2014), we present the X-ray crystal structure of an active MCM hexamer, which suggests a mechanism for MCM regulation and demonstrates a key interaction between the major domains.

Analysis of an essential motif in Mcm4 provides insights into replicative helicase double-hexamer formation and the first step requiring this intermediate during replication initiation.

Systematic analyses of DNA replication machinery components in human cells reveal a requirement of MCM-dependent de novo loading or mobilization of cohesin at replication forks in establishing sister-chromatid cohesion.

A multi-step process of helicase activation sensitizes replication initiation to the extent of replicative helicase phosphorylation.