A structural investigation reveals details of the mechanism by which the nuclease RecJ processes DNA ends to repair double strand breaks.

RecA is inactivated by oxidative stress and repaired by the MsrA/B anti-ROS defense system.

RecO efficiently displaces SSB from ssDNA without consuming ATPs using its two DNA-binding sites, even though SSB binds to ssDNA approximately 300 times more strongly than RecO does.

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

RecX effectively disrupts dynamic conformational changes in the RecA-ssDNA filament by stabilizing its inactive form.

A 3.1 Å structure of cytoplasmic dynein-1 in complex with its regulator Lis1 reveals the interfaces between dynein and Lis1, all of which are important for dynein function in vitro and in vivo.

The rate of DNA unwinding by RecQ helicases is dramatically modulated by the DNA duplex stability in a geometry-dependent manner, providing an intrinsic mechanism for suppressing illegitimate recombination.

Using a proximity-dependent labeling approach in living cells, the human cytoplasmic dynein-1 interactome was identified and a new family of dynein activators, ninein and ninein-like, was discovered.

DNA unwinding triggers a conformational change in the RecD subunit of E. coli RecBCD helicase-nuclease that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit.

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