Single-molecule force and fluorescence spectroscopy reveal the structural states and dynamics of E. coli single-stranded DNA binding proteins and the energy landscape of the nucleo–protein complex.

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

Individual SSB-ssDNA complexes undergo reversible condensation and de-condensation that is modulated by RecOR during recombination.

New cryoEM structures reveal how small bacteriophage proteins suppress bacterial immunity.

Biochemical and structural analyses reveal direct ubiquitin modification of single-stranded nucleic acids, catalysed by the DTX3L ubiquitin ligase.

Structural, biochemical, and cellular data reveal the mechanism by which the clamp loader attaches sliding clamps at gapped and nicked DNA to support DNA damage repair.

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.

In vivo single-molecule imaging demonstrates that Smc5/6 chromatin association depends on ATP hydrolysis and dsDNA binding, requires Nse6 and is modulated by Brc1 after DNA damage.

The role of the bacterial protein RadA in homologous recombination – a DNA repair pathway vital to all cells – is defined.

The tetrameric structure of a casposase bound to DNA and its biochemical properties show how a transposase could have evolved to perform CRISPR-Cas spacer acquisition.