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A single-stranded DNA binding protein stimulates helicase-mediated DNA unwinding by transiently activating a latent processivity switch in the helicase.

Single-molecule FRET experiments reveal that G40P, a DnaB-like helicase, unwinds double-stranded DNA in single base pair steps and its processivity is enhanced by host primase DnaG.

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

Integration of structural bioinformatics and free-energy simulations reveals how a helicase switches its function from unwinding to rezipping DNA, during which a key metastable conformation is predicted and verified by single-molecule measurements.

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.

Analyzing single molecules reveals that Pif1 family helicases periodically patrol DNA, which may explain this enzyme's ability to suppress genome instability at G-quadruplex motifs and transcriptional RNA-DNA hybrids (R-loops).

Structure-guided biochemistry defines how the coupling between nucleic acid substrate binding and ATPase activity is used by a molecular switch to load ring-shaped motor proteins onto single-stranded DNA.

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.

Topoisomerase VI selectively catalyzes strand passage of DNA molecules juxtaposed at close to a right angle, which explains the observed chiral-dependent activity and preferential DNA decatenation versus supercoil relaxation.

Human telomerase unfolds and extends parallel G-quadruplexes using a unique mechanism involving its RNA template.