The core domains of an RNA helicase interact with a wide variety of NTPs and nucleic acids suggesting how related enzymes may have evolved to have diverse functions.

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.

Analysis of the Escherichia coli DnaB helicase•bacteriophage λ helicase loader (λP) complex provides insights into helicase opening, delivery to the origin and ssDNA entry, and closing in preparation for translocation.

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.

A single origin–recognition complex (ORC) directs loading of a pair of head-to-head Mcm2-7 replicative DNA helicases by forming a protein tether to the first helicase, releasing from its initial DNA-binding site, and rebinding the origin DNA in the opposite orientation.

X-ray crystallography reveals that the Dna2 nuclease-helicase contains a long tunnel through which single-stranded DNA threads, and an allosteric mechanism for displacing the DNA-binding protein Rpa that restricts cleavage to the proper polarity.

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

The ability of an enzyme called XPD helicase to unwind the double helix is influenced by the DNA sequence and the availability of energy.

The structural and functional analysis of the ATP-dependent RNA helicase Prp43 provides insights into the mechanisms of RNA binding and translocation, which could serve as paradigm for all DEAH-box proteins.