ArticleBiochemistry2006
Saccharomyces cerevisiae replication protein A binds to single-stranded DNA in multiple salt-dependent modes.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 84 citations in OpenAlex.
- Two distinct Okazaki fragment failure modes dominate mutagenesis in the absence of flap endonuclease 1.Nature communications · 2026Article
- Mechanistic insights into direct DNA and RNA strand transfer and dynamic protein exchange of SSB and RPA.Nucleic acids research · 2025Article
- Targeting DNA damage sensors for cancer therapy.DNA repair · 2025Review
- Partial wrapping of single-stranded DNA by replication protein A and modulation through phosphorylation.Nucleic acids research · 2024Article
- Replication protein A dynamically re-organizes on primer/template junctions to permit DNA polymerase δ holoenzyme assembly and initiation of DNA synthesis.Nucleic acids research · 2024Article
- Wrapping of single-stranded DNA by Replication Protein A and modulation through phosphorylation.bioRxiv : the preprint server for biology · 2024Article
- Rapid Long-distance Migration of RPA on Single Stranded DNA Occurs Through Intersegmental Transfer Utilizing Multivalent Interactions.Journal of molecular biology · 2024Article
- Alteration of replication protein A binding mode on single-stranded DNA by NSMF potentiates RPA phosphorylation by ATR kinase.Nucleic acids research · 2023Article
- ssDNA accessibility of Rad51 is regulated by orchestrating multiple RPA dynamics.Nature communications · 2023Article
- Single-molecule visualization of Pif1 helicase translocation on single-stranded DNA.The Journal of biological chemistry · 2023Article
- "Helicase" Activity promoted through dynamic interactions between a ssDNA translocase and a diffusing SSB protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A DNA damage-induced phosphorylation circuit enhances Mec1Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Rtt105 regulates RPA function by configurationally stapling the flexible domains.Nature communications · 2022Article
- Hydrogen-deuterium exchange reveals a dynamic DNA-binding map of replication protein A.Nucleic acids research · 2021Article
- Understanding the Interaction of Polyelectrolyte Architectures with Proteins and Biosystems.Angewandte Chemie (International ed. in English) · 2021Review
- Unlimited Cooperativity ofFrontiers in microbiology · 2021Article
- Dynamic elements of replication protein A at the crossroads of DNA replication, recombination, and repair.Critical reviews in biochemistry and molecular biology · 2020Review
- Rad54 Drives ATP Hydrolysis-Dependent DNA Sequence Alignment during Homologous Recombination.Cell · 2020Article
- Dynamics of E. coli single stranded DNA binding (SSB) protein-DNA complexes.Seminars in cell & developmental biology · 2019Review
- Dynamics and selective remodeling of the DNA-binding domains of RPA.Nature structural & molecular biology · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have examined the single-stranded DNA (ssDNA) binding properties of the Saccharomyces cerevisiae replication protein A (scRPA) using fluorescence titrations, isothermal titration calorimetry, and sedimentation equilibrium to determine whether scRPA can bind to ssDNA in multiple binding modes. We measured the occluded site size for scRPA binding poly(dT), as well as the stoichiometry, equilibrium binding constants, and binding enthalpy of scRPA-(dT)L complexes as a function of the oligodeoxynucleotide length, L. Sedimentation equilibrium studies show that scRPA is a stable heterotrimer over the range of [NaCl] examined (0.02-1.5 M). However, the occluded site size, n, undergoes a salt-dependent transition between values of n = 18-20 nucleotides at low [NaCl] and values of n = 26-28 nucleotides at high [NaCl], with a transition midpoint near 0.36 M NaCl (25.0 degrees C, pH 8.1). Measurements of the stoichiometry of scRPA-(dT)L complexes also show a [NaCl]-dependent change in stoichiometry consistent with the observed change in the occluded site size. Measurements of the deltaH(obsd) for scRPA binding to (dT)L at 1.5 M NaCl yield a contact site size of 28 nucleotides, similar to the occluded site size determined at this [NaCl]. Altogether, these data support a model in which scRPA can bind to ssDNA in at least two binding modes, a low site size mode (n = 18 +/- 1 nucleotides), stabilized at low [NaCl], in which only three of its oligonucleotide/oligosaccharide binding folds (OB-folds) are used, and a higher site size mode (n = 27 +/- 1 nucleotides), stabilized at higher [NaCl], which uses four of its OB-folds. No evidence for highly cooperative binding of scRPA to ssDNA was found under any conditions examined. Thus, scRPA shows some behavior similar to that of the E. coli SSB homotetramer, which also shows binding mode transitions, but some significant differences also exist.
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