ArticleNucleic acids research2012
Highly organized DnaA-oriC complexes recruit the single-stranded DNA for replication initiation.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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Who cites it
81 citing papers in PubMed.
- Robust helicase loading mechanism underlies diverse architectures of bacterial replication origins.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
- The chromosomal origin of replication as the basis for the spatio-temporal biology of bacteria.Frontiers in microbiology · 2026Review
- Extrusion-modulated DnaA activity oscillations coordinate DNA replication with biomass growth.eLife · 2025Article
- Adaptive evolution of oriC through in vitro propagation of a mini-chromosome in RCR.Nucleic acids research · 2025Article
- Article
- How bacteria initiate DNA replication comes into focus.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- DnaA modulates the gene expression and morphology of the Lyme disease spirochete.bioRxiv : the preprint server for biology · 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
- 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
- Inhibition of Replication Fork Formation and Progression: Targeting the Replication Initiation and Primosomal Proteins.International journal of molecular sciences · 2023Review
- Borrelia burgdorferi DnaA and the Nucleoid-Associated Protein EbfC Coordinate Expression of theJournal of bacteriology · 2023Article
- Toward an understanding of the DNA replication initiation in bacteria.Frontiers in microbiology · 2023Review
- The Caulobacter crescentus DciA promotes chromosome replication through topological loading of the DnaB replicative helicase at replication forks.Nucleic acids research · 2022Article
- HU Knew? Bacillus subtilis HBsu Is Required for DNA Replication Initiation.Journal of bacteriology · 2022Article
- Concerted actions of DnaA complexes with DNA-unwinding sequences within and flanking replication origin oriC promote DnaB helicase loading.The Journal of biological chemistry · 2022Article
21 more citing papers are in PubMed but not listed here.
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2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, the replication origin oriC consists of two functional regions: the duplex unwinding element (DUE) and its flanking DnaA-assembly region (DAR). ATP-DnaA molecules multimerize on DAR, unwinding DUE for DnaB helicase loading. However, DUE-unwinding mechanisms and functional structures in DnaA-oriC complexes supporting those remain unclear. Here, using various in vitro reconstituted systems, we identify functionally distinct DnaA sub-complexes formed on DAR and reveal novel mechanisms in DUE unwinding. The DUE-flanking left-half DAR carrying high-affinity DnaA box R1 and the ATP-DnaA-preferential DnaA box R5, τ1-2 and I1-2 sites formed a DnaA sub-complex competent in DUE unwinding and ssDUE binding, thereby supporting basal DnaB loading activity. This sub-complex is further subdivided into two; the DUE-distal DnaA sub-complex formed on the ATP-DnaA-preferential sites binds ssDUE. Notably, the DUE-flanking, DnaA box R1-DnaA sub-complex recruits DUE to the DUE-distal DnaA sub-complex in concert with a DNA-bending nucleoid protein IHF, thereby promoting DUE unwinding and binding of ssDUE. The right-half DAR-DnaA sub-complex stimulated DnaB loading, consistent with in vivo analyses. Similar features are seen in DUE unwinding of the hyperthermophile, Thermotoga maritima, indicating evolutional conservation of those mechanisms.
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