ArticleMolecular and cellular biology1998
Identification and characterization of the fourth single-stranded-DNA binding domain of replication protein A.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
41 citing papers in PubMed, 88 citations in OpenAlex.
- Mechanistic insights into direct DNA and RNA strand transfer and dynamic protein exchange of SSB and RPA.Nucleic acids research · 2025Article
- Exploring the structural landscape of DNA maintenance proteins.Nature communications · 2024Article
- DNA-binding mechanism and evolution of replication protein A.Nature communications · 2023Article
- Distinct RPA domains promote recruitment and the helicase-nuclease activities of Dna2.Nature communications · 2021Article
- The Essential, Ubiquitous Single-Stranded DNA-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Dynamic elements of replication protein A at the crossroads of DNA replication, recombination, and repair.Critical reviews in biochemistry and molecular biology · 2020Review
- Monitoring Replication Protein A (RPA) dynamics in homologous recombination through site-specific incorporation of non-canonical amino acids.Nucleic acids research · 2017Article
- A data-driven structural model of hSSB1 (NABP2/OBFC2B) self-oligomerization.Nucleic acids research · 2017Article
- Recent advancements in the discovery of protein-protein interaction inhibitors of replication protein A.MedChemComm · 2017Review
- Dynamic binding of replication protein a is required for DNA repair.Nucleic acids research · 2016Article
- Replication protein A prevents promiscuous annealing between short sequence homologies: Implications for genome integrity.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Review
- RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage response.Cell research · 2015Review
- Diffusion of human replication protein A along single-stranded DNA.Journal of molecular biology · 2014Article
- Concentration-dependent exchange of replication protein A on single-stranded DNA revealed by single-molecule imaging.PloS one · 2014Article
- Structure and conformational change of a replication protein A heterotrimer bound to ssDNA.Genes & development · 2012Article
- Repair-specific functions of replication protein A.The Journal of biological chemistry · 2012Article
- The karyopherin Kap95 and the C-termini of Rfa1, Rfa2, and Rfa3 are necessary for efficient nuclear import of functional RPA complex proteins in Saccharomyces cerevisiae.DNA and cell biology · 2011Article
- Small molecule inhibitor of the RPA70 N-terminal protein interaction domain discovered using in silico and in vitro methods.Bioorganic & medicinal chemistry · 2011Article
- Replication protein A: directing traffic at the intersection of replication and repair.Frontiers in bioscience (Landmark edition) · 2010Review
- Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA.Nucleic acids research · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Replication protein A (RPA), the heterotrimeric single-stranded-DNA (ssDNA) binding protein (SSB) of eukaryotes, contains two homologous ssDNA binding domains (A and B) in its largest subunit, RPA1, and a third domain in its second-largest subunit, RPA2. Here we report that Saccharomyces cerevisiae RPA1 contains a previously undetected ssDNA binding domain (domain C) lying in tandem with domains A and B. The carboxy-terminal portion of domain C shows sequence similarity to domains A and B and to the region of RPA2 that binds ssDNA (domain D). The aromatic residues in domains A and B that are known to stack with the ssDNA bases are conserved in domain C, and as in domain A, one of these is required for viability in yeast. Interestingly, the amino-terminal portion of domain C contains a putative Cys4-type zinc-binding motif similar to that of another prokaryotic SSB, T4 gp32. We demonstrate that the ssDNA binding activity of domain C is uniquely sensitive to cysteine modification but that, as with gp32, ssDNA binding is not strictly dependent on zinc. The RPA heterotrimer is thus composed of at least four ssDNA binding domains and exhibits features of both bacterial and phage SSBs.
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Registered trials
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