ArticleNucleic acids research2023
Distinct RPA functions promote eukaryotic DNA replication initiation and elongation.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Single-molecule DNA flow-stretch assays for high-throughput DNA-protein interaction studies.FEBS open bio · 2026Article
- A CRISPR-assisted passive microfluidic chip for rapid, visual detection of multiple respiratory viruses.Scientific reports · 2025Article
- RNA polymerase II is a polar roadblock to a progressing DNA fork.Nature communications · 2025Article
- RPA1 protects DNA damage-induced PANoptosis in limb development.Science advances · 2025Article
- The human primosome requires replication protein A when copying DNA with inverted repeats.Nucleic acids research · 2025Article
- Aere perennius: how chromatin fidelity is maintained and lost in disease.NAR molecular medicine · 2025Review
- Mechanistic insights into direct DNA and RNA strand transfer and dynamic protein exchange of SSB and RPA.Nucleic acids research · 2025Article
- The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Communication between DNA polymerases and Replication Protein A within the archaeal replisome.Nature communications · 2024Article
- Guardians of the Genome: How the Single-Stranded DNA-Binding Proteins RPA and CST Facilitate Telomere Replication.Biomolecules · 2024Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Replication protein A (RPA) binds single-stranded DNA (ssDNA) and serves critical functions in eukaryotic DNA replication, the DNA damage response, and DNA repair. During DNA replication, RPA is required for extended origin DNA unwinding and DNA synthesis. To determine the requirements for RPA during these processes, we tested ssDNA-binding proteins (SSBs) from different domains of life in reconstituted Saccharomyces cerevisiae origin unwinding and DNA replication reactions. Interestingly, Escherichia coli SSB, but not T4 bacteriophage Gp32, fully substitutes for RPA in promoting origin DNA unwinding. Using RPA mutants, we demonstrated that specific ssDNA-binding properties of RPA are required for origin unwinding but that its protein-interaction domains are dispensable. In contrast, we found that each of these auxiliary RPA domains have distinct functions at the eukaryotic replication fork. The Rfa1 OB-F domain negatively regulates lagging-strand synthesis, while the Rfa2 winged-helix domain stimulates nascent strand initiation. Together, our findings reveal a requirement for specific modes of ssDNA binding in the transition to extensive origin DNA unwinding and identify RPA domains that differentially impact replication fork function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.