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.

Genetic and physical analyses reveal that DNA-RNA hybrids form fortuitously at DNA double-strand breaks during transcription and need removal to allow repair by homologous 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.

The long-range resection machinery is dispensable for homologous recombination between closely linked repeats but is necessary for DNA damage checkpoint activation which is associated with interchromosomal recombination.

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.

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 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.

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.

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

When a protein involved in DNA repair malfunctions, it can anneal RNA molecules to DNA molecules, creating hybrids that increase the frequency of mutations in the DNA.