Replication protein A as a major eukaryotic single-stranded DNA-binding protein and its role in DNA repair

• Published in: Molecular biology (New York) Vol. 50; no. 5; pp. 649 - 662
• Main Authors: Krasikova, Y. S., Rechkunova, N. I., Lavrik, O. I.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.09.2016; Springer Nature B.V
• Subjects: Biochemistry; Biomedical and Life Sciences; Deoxyribonucleic acid; DNA; DNA biosynthesis; DNA damage; DNA repair; DNA structure; DNA-binding protein; Human Genetics; Intermediates; Life Sciences; Metabolic pathways; Metabolism; Oligonucleotides; Protein A; Protein structure; Proteins; Recombination; Replication; Replication protein A; Reviews; Secondary structure; Single-stranded DNA; Single-stranded DNA-binding protein; replication protein A; DNA repair; DNA replication
• ISSN: 0026-8933; 1608-3245
• DOI: 10.1134/S0026893316030080

Replication protein A (RPA) is a key regulator of eukaryotic DNA metabolism. RPA is a highly conserved heterotrimeric protein and contains multiple oligonucleotide/oligosaccharide-binding folds. The major RPA function is binding to single-stranded DNA (ssDNA) intermediates forming in DNA replication, repair, and recombination. Although binding ssDNA with high affinity, RPA can rapidly diffuse along ssDNA and destabilizes the DNA secondary structure. A highly dynamic RPA binding to ssDNA allows other proteins to access ssDNA and to displace RPA from the RPA–ssDNA complex. As has been shown recently, RPA in complex with ssDNA is posttranslationally modified in response to DNA damage. These modifications modulate the RPA interactions with its protein partners and control the DNA damage signaling pathways. The review considers up-to-date data on the RPA function as an active coordinator of ssDNA intermediate processing within DNA metabolic pathways, DNA repair in particular.