ArticleNucleic acids research2021
Multiprotein E. coli SSB-ssDNA complex shows both stable binding and rapid dissociation due to interprotein interactions.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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Who cites it
30 citing papers in PubMed, 38 citations in OpenAlex.
- Azure A Dye Interaction with Double-Stranded DNA Can Be Modulated by the Ionic Strength: Choosing the Binding Mode.ACS omega · 2026Article
- Characterizing Complex Nucleic Acid Interactions of LINE1 ORF1p by Single-Molecule Force Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Genome integrity relies on rapid recycling of DNA Pol III in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The YoaA-χ helicase modulates the dynamics of single-stranded DNA binding protein on DNA.Nature communications · 2025Article
- Diverse single-stranded nucleic acid binding proteins enable both stable protection and rapid exchange required for biological function.QRB discovery · 2025Article
- L1-ORF1p nucleoprotein can rapidly assume distinct conformations and simultaneously bind more than one nucleic acid.Nucleic acids research · 2024Article
- Single-stranded DNA binding protein hitches a ride with thebioRxiv : the preprint server for biology · 2024Article
- Escherichia coli DNA replication: the old model organism still holds many surprises.FEMS microbiology reviews · 2024Review
- The mutation R107Q alters mtSSB ssDNA compaction ability and binding dynamics.Nucleic acids research · 2024Article
- Article
- HIV-1 uncoating requires long double-stranded reverse transcription products.Science advances · 2024Article
- Stochastic nucleosome disassembly mediated by remodelers and histone fragmentation.The Journal of chemical physics · 2023Article
- Distinct RPA functions promote eukaryotic DNA replication initiation and elongation.Nucleic acids research · 2023Article
- DNA damage alters binding conformations of E. coli single-stranded DNA-binding protein.Biophysical journal · 2023Article
- Dynamic structure of T4 gene 32 protein filaments facilitates rapid noncooperative protein dissociation.Nucleic acids research · 2023Article
- Single-molecule imaging of genome maintenance proteins encountering specific DNA sequences and structures.DNA repair · 2023Review
- Regulation of T7 gp2.5 binding dynamics by its C-terminal tail, template conformation and sequence.Nucleic acids research · 2023Article
- ssDNA accessibility of Rad51 is regulated by orchestrating multiple RPA dynamics.Nature communications · 2023Article
- Mechanism of strand displacement DNA synthesis by the coordinated activities of human mitochondrial DNA polymerase and SSB.Nucleic acids research · 2023Article
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli SSB (EcSSB) is a model single-stranded DNA (ssDNA) binding protein critical in genome maintenance. EcSSB forms homotetramers that wrap ssDNA in multiple conformations to facilitate DNA replication and repair. Here we measure the binding and wrapping of many EcSSB proteins to a single long ssDNA substrate held at fixed tensions. We show EcSSB binds in a biphasic manner, where initial wrapping events are followed by unwrapping events as ssDNA-bound protein density passes critical saturation and high free protein concentration increases the fraction of EcSSBs in less-wrapped conformations. By destabilizing EcSSB wrapping through increased substrate tension, decreased substrate length, and protein mutation, we also directly observe an unstable bound but unwrapped state in which ∼8 nucleotides of ssDNA are bound by a single domain, which could act as a transition state through which rapid reorganization of the EcSSB-ssDNA complex occurs. When ssDNA is over-saturated, stimulated dissociation rapidly removes excess EcSSB, leaving an array of stably-wrapped complexes. These results provide a mechanism through which otherwise stably bound and wrapped EcSSB tetramers are rapidly removed from ssDNA to allow for DNA maintenance and replication functions, while still fully protecting ssDNA over a wide range of protein concentrations.
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