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.

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.

Small molecule inhibitors identified in a biophysical high-throughout screening assay confirm the importance of the interaction between single-stranded DNA and the protein RAD52 for the survival of BRCA2-depleted cells.

The association of Rad52 with Rad51, while not critical for Rad51 filament formation, is crucial to protect Rad51 filaments from Srs2 translocase activity through the association of Rad52 with complete Rad51 filaments.

The mechanism of Dbf4-dependent kinase (DDK) recruitment to replication origins and its regulation by the checkpoint have been identified.

DNA replication fork rate in budding yeast is regulated in response to DNA damage by phosphorylation of two proteins, Mrc1 and Mcm10, by the Rad53 protein kinase.

The dsDNA-dependent motor protein Rdh54 antagonizes Rad51-Rad54-mediated D-loop formation during homologous recombination and restricts the length of D-loops.

RNA does not form DNA:RNA hybrids in trans that compromise genome integrity.

p53 suppresses genome instability by direct role at stalled replication forks for pathway regulation that explains transcription-independent p53 tumor-suppressor functions.

Upon DNA damage, Rad52 forms a membraneless sub-compartment where Rad52 molecules are highly dynamic and share properties with liquid-liquid phase-separated molecules, reflecting the existence of a liquid droplet around damaged DNA.