ArticleThe Journal of biological chemistry2008
Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA).
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 41 citations in OpenAlex.
- Genome-wide mapping of replication stress response factors reveals the management of polycistronic transcription, replication initiation, and responses to replication stress in Leishmania.Nucleic acids research · 2026Article
- The effect of replication protein A inhibition and post-translational modification on ATR kinase signaling.Scientific reports · 2024Article
- The Effect of Replication Protein A Inhibition and Post-Translational Modification on ATR Kinase Signaling.Research square · 2024Article
- RPA interacts with Rad52 to promote meiotic crossover and noncrossover recombination.Nucleic acids research · 2024Article
- Replication Protein A, the Main Eukaryotic Single-Stranded DNA Binding Protein, a Focal Point in Cellular DNA Metabolism.International journal of molecular sciences · 2024Review
- Phase separation properties of RPA combine high-affinity ssDNA binding with dynamic condensate functions at telomeres.Nature structural & molecular biology · 2023Article
- Deciphering the mechanism of processive ssDNA digestion by the Dna2-RPA ensemble.Nature communications · 2022Article
- OB-Folds and Genome Maintenance: Targeting Protein-DNA Interactions for Cancer Therapy.Cancers · 2021Review
- The Essential, Ubiquitous Single-Stranded DNA-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Determinants of replication protein A subunit interactions revealed using a phosphomimetic peptide.The Journal of biological chemistry · 2020Article
- Large-scale contractions of Friedreich's ataxia GAA repeats in yeast occur during DNA replication due to their triplex-forming ability.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- RPA Phosphorylation Inhibits DNA Resection.Molecular cell · 2019Article
- Dynamic binding of replication protein a is required for DNA repair.Nucleic acids research · 2016Article
- Single-molecule imaging reveals the mechanism of Exo1 regulation by single-stranded DNA binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response.Cell research · 2015Review
- Replication protein A: single-stranded DNA's first responder: dynamic DNA-interactions allow replication protein A to direct single-strand DNA intermediates into different pathways for synthesis or repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2014Review
- Rfa2 is specifically dephosphorylated by Pph3 in Candida albicans.The Biochemical journal · 2013Article
- In vitro analysis of the role of replication protein A (RPA) and RPA phosphorylation in ATR-mediated checkpoint signaling.The Journal of biological chemistry · 2012Article
- Repair-specific functions of replication protein A.The Journal of biological chemistry · 2012Article
- Opposing role of condensin hinge against replication protein A in mitosis and interphase through promoting DNA annealing.Open biology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Replication protein A (RPA) is the major single-stranded DNA-binding protein in eukaryotes. RPA is composed of three subunits of 70, 32, and 14 kDa. The N-terminal domain of the 70-kDa subunit (RPA70) has weak DNA binding activity, interacts with proteins, and is involved in cellular DNA damage response. To define the mechanism by which this domain regulates RPA function, we analyzed the function of RPA forms containing a deletion of the N terminus of RPA70 and mutations in the phosphorylation domain of RPA (N-terminal 40 amino acids of the 32-kDa subunit). Although each individual mutation has only modest effects on RPA activity, a form combining both phosphorylation mimetic mutations and a deletion of the N-terminal domain of RPA70 was found to have dramatically altered activity. This combined mutant was defective in binding to short single-stranded DNA oligonucleotides and had altered interactions with proteins that bind to the DNA-binding core of RPA70. These results indicate that in the absence of the N-terminal domain of RPA70, a negatively charged phosphorylation domain disrupts the activity of the core DNA-binding domain of RPA. We conclude that the N-terminal domain of RPA70 functions by interacting with the phosphorylation domain of the 32-kDa subunit and blocking undesirable interactions with the core DNA-binding domain of RPA. These studies indicate that RPA conformation is important for regulating RPA-DNA and RPA-protein interactions.
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