ArticleNucleic acids research2017
Regulatory dynamics in the ternary DnaA complex for initiation of chromosomal replication in Escherichia coli.
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 41 papers.
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41 citing papers in PubMed.
- Robust helicase loading mechanism underlies diverse architectures of bacterial replication origins.Nucleic acids research · 2026Article
- Structures of DnaA domain I reveal a dimer conserved across Actinomycetes.Nucleic acids research · 2026Article
- Dynamic DnaA-DnaB interactions at oriC coordinate the loading and coupled translocation of two DnaB helicases for bidirectional replication.Nucleic acids research · 2026Article
- Mechanisms of chromosomal DNA replication in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2026Review
- Phosphodiesterase BpdE suppress bacterial proliferation by regulatingFrontiers in microbiology · 2026Article
- The chromosomal origin of replication as the basis for the spatio-temporal biology of bacteria.Frontiers in microbiology · 2026Review
- An Orc1 initiator-specific motif (ISM)-related region limits ORC-ssDNA binding and promotes replication origin specificity in budding yeast.Frontiers in microbiology · 2026Article
- Adaptive evolution of oriC through in vitro propagation of a mini-chromosome in RCR.Nucleic acids research · 2025Article
- Article
- Review
- Negative DNA supercoiling enhances DARS2 binding of DNA-bending protein IHF in the activation of Fis-dependent ATP-DnaA production.Nucleic acids research · 2025Article
- How bacteria initiate DNA replication comes into focus.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Read-through transcription of tRNA underlies the cell cycle-dependent dissociation of IHF from the DnaA-inactivating sequenceFrontiers in microbiology · 2024Article
- The bacterial replication origin BUS promotes nucleobase capture.Nature communications · 2023Article
- Cell cycle-coordinated maintenance of theEcoSal Plus · 2023Review
- Rep protein accommodates together dsDNA and ssDNA which enables a loop-back mechanism to plasmid DNA replication initiation.Nucleic acids research · 2023Article
- Open Questions about the Roles of DnaA, Related Proteins, and Hyperstructure Dynamics in the Cell Cycle.Life (Basel, Switzerland) · 2023Review
- IHF and Fis asInternational journal of molecular sciences · 2023Review
- Single-stranded DNA recruitment mechanism in replication origin unwinding by DnaA initiator protein and HU, an evolutionary ubiquitous nucleoid protein.Nucleic acids research · 2023Article
- Toward an understanding of the DNA replication initiation in bacteria.Frontiers in microbiology · 2023Review
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5 authors.
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Abstract
In Escherichia coli, the level of the ATP-DnaA initiator is increased temporarily at the time of replication initiation. The replication origin, oriC, contains a duplex-unwinding element (DUE) flanking a DnaA-oligomerization region (DOR), which includes twelve DnaA-binding sites (DnaA boxes) and the DNA-bending protein IHF-binding site (IBS). Although complexes of IHF and ATP-DnaA assembly on the DOR unwind the DUE, the configuration of the crucial nucleoprotein complexes remains elusive. To resolve this, we analyzed individual DnaA protomers in the complex and here demonstrate that the DUE-DnaA-box-R1-IBS-DnaA-box-R5M region is essential for DUE unwinding. R5M-bound ATP-DnaA predominantly promotes ATP-DnaA assembly on the DUE-proximal DOR, and R1-bound DnaA has a supporting role. This mechanism might support timely assembly of ATP-DnaA on oriC. DnaA protomers bound to R1 and R5M directly bind to the unwound DUE strand, which is crucial in replication initiation. Data from in vivo experiments support these results. We propose that the DnaA assembly on the IHF-bent DOR directly binds to the unwound DUE strand, and timely formation of this ternary complex regulates replication initiation. Structural features of oriC support the idea that these mechanisms for DUE unwinding are fundamentally conserved in various bacterial species including pathogens.
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