Genome-wide mapping of heteroduplex DNA (a recombination intermediate) formed during mitotic recombination in yeast demonstrates that the "classical" model of double-strand DNA break repair is inadequate to explain several aspects of mitotic recombination.

DNA-bound crystal structures of an essential Xer site-specific recombinase from the bacterium Helicobacter pylori reveal how large conformational changes initiate the untangling of chromosomes upon cell division.

A new mechanism is uncovered by which the RNF168 ubiquitin ligase couples PALB2-dependent homologous recombination to H2A ubiquitylation to promote DNA repair and preserve genome integrity.

The structure of the recombination complex responsible for flagellar antigen switching in Salmonella enterica, and the mechanism that regulates the site-specific DNA inversion reaction, have been determined.

Although Rad51 is the central protein involved in recombinational DNA repair, multiple auxiliary factors potentiate its activity by binding to a single, evolutionarily conserved motif.

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

In humans, specific sequence features can predict whether meiotic recombination occurs at sites bound by the protein PRDM9, whose DNA-binding zinc-finger domain can unexpectedly bind to gene promoters and to other copies of PRDM9.

Random sequence RNA pools display an innate capacity for ligation and recombination, enabling them to “bootstrap” themselves towards higher compositional, informational and structural complexity.

Unloading the polymerase sliding clamp PCNA from DNA by Elg1 promotes recombination at the RTS1 replication fork barrier by limiting Fbh1 and Srs2 activity.

The intrinsically disordered N-terminus of Sfr1 contains two Rad51 binding sites that facilitate Rad51 filament stabilization and ATPase stimulation by the Swi5-Sfr1 complex, leading to efficient Rad51-driven strand exchange.