The human RAD52 complex undergoes phase separation and facilitates bundling and end-to-end tethering of RAD51 presynaptic filaments.

ABSTRACT: Human RAD52 is a prime target for synthetic lethality approaches to treat cancers with deficiency in homologous recombination. Among multiple cellular roles, RAD52's functions in homologous recombination repair and stalled replication fork protection appear to substitute for those of the tumor suppressor protein BRCA2. However, the mechanistic details of how RAD52 substitutes for BRCA2 functions are only beginning to emerge. RAD52 forms an oligomeric ring enveloped by ∼200-residue-long disordered regions, forming a highly multivalent and branched protein complex that promotes supramolecular assembly. Here, we demonstrate that RAD52 undergoes homotypic phase separation, forming condensates that recruit key homologous recombination factors, including single-stranded DNA (ssDNA), replication

SUBMITTER: Alshareedah I 

PROVIDER: S-EPMC12848948 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature