Homologous recombination (HR) plays a vital role in DNA metabolic processes including meiosis, DNA repair, DNA replication, and maintenance of rDNA homeostasis. Defects in HR can lead to pathological outcomes, including genetic diseases and cancer. Recent studies suggest that the post-translational modification by small ubiquitin-like modifier (SUMO) protein plays an important role in mitotic and meiotic recombination. We find that SUMOylation can significantly influence the biochemical properties of the modified proteins as well as their localization. The precise role of SUMOylation during recombination and DNA repair is still indistinct. Characterization of the novel effect of SUMOylation on the properties of Saccharomyces cerevisiae mediator protein Rad52 will be presented and the model for the recombination quality control discussed.