ArticleNucleic acids research2017
Dynamic stepwise opening of integron attC DNA hairpins by SSB prevents toxicity and ensures functionality.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Slippage reconfiguration of trinucleotide repeat hairpins impedes resolution by human replication protein A.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Diverse single-stranded nucleic acid binding proteins enable both stable protection and rapid exchange required for biological function.QRB discovery · 2025Article
- The recombination efficiency of the bacterial integron depends on the mechanical stability of the synaptic complex.Science advances · 2024Article
- Chromosomal integrons are genetically and functionally isolated units of genomes.Nucleic acids research · 2024Article
- An automated single-molecule FRET platform for high-content, multiwell plate screening of biomolecular conformations and dynamics.Nature communications · 2023Article
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
- Article
- A blind benchmark of analysis tools to infer kinetic rate constants from single-molecule FRET trajectories.Nature communications · 2022Article
- Unbridled Integrons: A Matter of Host Factors.Cells · 2022Review
- Article
- Multiprotein E. coli SSB-ssDNA complex shows both stable binding and rapid dissociation due to interprotein interactions.Nucleic acids research · 2021Article
- Structure-specific DNA recombination sites: Design, validation, and machine learning-based refinement.Science advances · 2020Article
- Structural heterogeneity of attC integron recombination sites revealed by optical tweezers.Nucleic acids research · 2019Article
- Polymorphisms of Gene Cassette Promoters of the Class 1 Integron in ClinicalFrontiers in microbiology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biologically functional DNA hairpins are found in archaea, prokaryotes and eukaryotes, playing essential roles in various DNA transactions. However, during DNA replication, hairpin formation can stall the polymerase and is therefore prevented by the single-stranded DNA binding protein (SSB). Here, we address the question how hairpins maintain their functional secondary structure despite SSB's presence. As a model hairpin, we used the recombinogenic form of the attC site, essential for capturing antibiotic-resistance genes in the integrons of bacteria. We found that attC hairpins have a conserved high GC-content near their apical loop that creates a dynamic equilibrium between attC fully opened by SSB and a partially structured attC-6-SSB complex. This complex is recognized by the recombinase IntI, which extrudes the hairpin upon binding while displacing SSB. We anticipate that this intriguing regulation mechanism using a base pair distribution to balance hairpin structure formation and genetic stability is key to the dissemination of antibiotic resistance genes among bacteria and might be conserved among other functional hairpins.
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