[4]  DBDs C, D, and E make up the trimerization core of the protein with flexible linker regions connecting them all together.

Because of this dynamic binding, RPA is also capable of different conformations that leads to varied numbers of nucleotides that it can engage.

RPA also binds to ssDNA during the initial phase of homologous recombination, an important process in DNA repair and prophase I of meiosis.

RPA has a key role in the maintenance of the recombination checkpoint during meiosis of the yeast Saccharomyces cerevisiae.

[8] Like its role in DNA replication, this keeps ssDNA from binding to itself (self-complementizing) so that the resulting nucleoprotein filament can then be bound by Rad51 and its cofactors.