A PTM known as sumoylation, manifested by an attachment of a SUMO molecule (small ubiquition-like modifier) to target proteins, may lead to changes in the tagged protein’s function, localization or stability. This PTM is present in all eukaryotes. In fission yeast, Rad52 is a DNA repair mediator protein, which enables stalled replicatory fork restart via a homologous recombination mechanism. Fork stalling was postulated to rely on the so-called SUMOylation waves of certain replisome components. Within the project we aimed to identify the protein content at the Rad52-dependent repair sites, which undergo a SUMO wave event. For this purpose, a peculiar proximity labelling approach was uptaken, which is based on fusing two interaction partners to distinct domains (N and C terminal) of a TurboID biotin ligase. Only upon partners’ contact, the ligase is reconstituted and active to label nearby proteins with a biotin molecule, hence providing elusive means of specifically capturing interaction-dependent interactomes.