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Nucleosomal DNAs assembled or modified by different chromatin remodeling enzymes differentially impact the origin licensing and helicase activation steps of replication initiation.

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.

UPF1 associates with nascent transcripts and plays a broad role in nuclear processes of gene expression.

A phage-encoded protein inhibits a bacterial replicative helicase loading factor by exploiting an internal site that auto-regulates loader self-assembly and ATPase activity.

DNA unwinding triggers a conformational change in the RecD subunit of E. coli RecBCD helicase-nuclease that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit.

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.

Ubiquitylation of the CMG helicase is inhibited throughout the initiation and elongation phases of chromosome replication by the DNA structure of a replication fork.

Utilizing a conserved mechanism, a ribosome can initiate translation from a site within the insulin receptor mRNA to maintain protein synthesis even when standard mechanisms of initiating translation have been inhibited by stress.

A new optical tweezers assay sheds light on the mechanism of cooperation and force generation by the subunits of RecBCD, critical for the repair of double strand breaks in bacteria.

RNA polymerase recruits the PcrA DNA helicase via a conserved interaction motif in order to remove R-loops and prevent conflicts with replication.