Abstract 2608 Computational analysis to follow the impact of phosphorylation at key serines in the intrinsically disordered C-terminal domain of the S. cerevisiae Srs2 helicase

The Srs2 helicase is an ATP-dependent translocase and helicase acting in primarily the 3'-5' direction and an anti-recombinase via direct interaction of its C-terminal domain (CTD) with Rad51 protein. It also helps to down-regulate the DNA damage checkpoint in cellular adaptation and promote gap repair, replication-restart, and translesion DNA synthesis through protein-protein interactions such as with PCNA-SUMO. The N-terminal region (776 residues) is structurally and functionally homologous with other SF-1 helicases, i.e.