Replication protein A: directing traffic at the intersection of replication and repair

Abstract

Since the initial discovery of replication protein A (RPA) as a DNA replication factor, much progress has been made on elucidating critical roles for RPA in other DNA metabolic pathways. RPA has been shown to be required for DNA replication, DNA repair, DNA recombination, and the DNA damage response pathway with roles in checkpoint activation. This review summarizes the current understanding of RPA structure, phosphorylation and protein-protein interactions in mediating these DNA metabolic processes.

Figure 1

RPA2 phosphorylation sites. N-terminal residues 1-34 are shown. Indicated above the sequence are sites for which phospho-specific antibodies are available. The putative kinases responsible for phosphorylation of specific residues are shown below the sequence.

Figure 2

Sequence alignment of identified and putative peptide sequences that bind to the N-terminal domain of RPA1.