Description
This protein removes 5 overhanging flaps in DNA repair and processes the 5 ends of Okazaki fragments in lagging strand DNA synthesis. Direct physical interaction between this protein and AP endonuclease 1 during long-patch base excision repair provides coordinated loading of the proteins onto the substrate, thus passing the substrate from one enzyme to another. The protein is a member of the XPG
RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5 end of the flap that is necessary for both binding and cleavage by This protein. Therefore, secondary structure can deter the protective function of this protein, leading to site-specific trinucleotide expansions