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.
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 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.
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.
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.
The role of the Frazzled chemoattractant receptor is to triggers migration initiation as part of the glial developmental program induced by the Glide/Gcm transcription factor.
The archaeal MCM helicase can load in multiple orientations on DNA but translocation proceeds with a leading N-terminal domain, which affects double hexamer activation at origins of replication.
New transgenic mice, which can be ablated both orexin neurons and MCH neurons, showed new brain state and revealed functional interaction that MCH neurons have protective role in narcolepsy symptoms.
Cell-cell junctions and the actin cytoskeleton are key players in the organisation and patterning of the extracellular matrix (ECM) on the apical side of tracheal cells.
