LIG_RPA_C_Fungi

Replication protein A (RPA) is a conserved eukaryotic single stranded DNA (ssDNA) binding protein and essential for DNA replication, recombination and repair. RPA consists of three subunits RPA70, RPA32 and RPA14, named after their molecular weight 70, 32 and 14 kDa, that form a stable complex (Fanning,2006). All three subunits consist primarily of OB fold domains that form the trimrization core and are responsible for ssDNA binding. Furthermore RPA70 N-terminal domain and RPA32 C-terminal domain can recruit a variety of DNA processing proteins in response to genomic stress and DNA damage (Xie,2014). The C terminus of subunit RPA32 contains a specific surface that interacts with a variety of DNA damage response proteins and therefore this region is required for base excision repair, nucleotide excision repair and S-phase checkpoint activation. RPA32C mediating the assembly of DNA repair complexes via a hand-off mechanism. In early steps of nucleotide excision repair and the repair of double-strand breaks by homologous recombination, RPA binds to the ssDNA opposite or adjacent to the site of DNA damage and interacts with one of the damage-recognition proteins (Mer,2000).