(Frontiers in Bioscience 15, 883-900, June 1, 2010)

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

Greg G. Oakley1, Steve M. Patrick2

1College of Dentistry, University of Nebraska Medical Center, Lincoln, Nebraska 68583, 2Department of Biochemistry and Cancer Biology, University of Toledo Medical Center, Toledo, Ohio 43614

TABLE OF CONTENTS

1. Abstract
2. Introduction
3. RPA structure and function
3.1. Protein structure and DNA binding domains
3.2. DNA binding and polarity
3.3. Phosphorylation of RPA2
3.4. Protein-protein interactions
4. RPA in DNA replication
5. RPA in DNA repair
5.1. Nucleotide excision repair
5.2. Base excision repair
5.3. Mismatch repair
5.4. DNA double-strand breaks and recombination
5.5. Telomere maintenance
6. Roles of RPA phosphorylation in the DNA damage response and checkpoint activation
7. Concluding remarks
8. Acknowledgements
9. References

1. 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.