RPA associates with ssDNA in distinct complexes that can be distinguished by the length of ssDNA occluded by each RPA molecule. These complexes reflect the progressive association of distinct DNA-binding domains present in the RPA heterotrimeric structure. Binding is coupled to significant conformational changes within RPA that are observable at the microscopic level. Presumably, the different conformations of free and ssDNA-bound RPA allow the protein to selectively interact with factors such as ATR-ATRIP when bound to DNA.
Golub, EI, Haaf, T, Raderschall, E
Walter, JC, Pacek, M, Byun, TS, Yee, MC, Cimprich, KA
Borowiec, JA, Blackwell, LJ
Zaritskaya, LS, Makhov, AM, Griffith, JD, Cordeiro-Stone, M
© 2025 Reactome