ArticleProceedings of the National Academy of Sciences of the United States of America2016
Near-atomic structural model for bacterial DNA replication initiation complex and its functional insights.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 55 citations in OpenAlex.
- 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
- 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
- NMR assignment of the conserved bacterial DNA replication protein DnaA domain IV.Biomolecular NMR assignments · 2024Article
- Dispensability of extrinsic DnaA regulators inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- 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
- 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
- Dynamics of chromosome organization in a minimal bacterial cell.Frontiers in cell and developmental biology · 2023Article
- Extracting time series matching a small-angle X-ray scattering profile from trajectories of molecular dynamics simulations.Scientific reports · 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
- Negative feedback for DARS2-Fis complex by ATP-DnaA supports the cell cycle-coordinated regulation for chromosome replication.Nucleic acids research · 2021Article
- Putative Cooperative ATP-DnaA Binding to Double-Stranded DnaA Box and Single-Stranded DnaA-Trio Motif uponInternational journal of molecular sciences · 2021Article
- Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation.Scientific reports · 2021Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon DNA replication initiation in Escherichia coli, the initiator protein DnaA forms higher-order complexes with the chromosomal origin oriC and a DNA-bending protein IHF. Although tertiary structures of DnaA and IHF have previously been elucidated, dynamic structures of oriC-DnaA-IHF complexes remain unknown. Here, combining computer simulations with biochemical assays, we obtained models at almost-atomic resolution for the central part of the oriC-DnaA-IHF complex. This complex can be divided into three subcomplexes; the left and right subcomplexes include pentameric DnaA bound in a head-to-tail manner and the middle subcomplex contains only a single DnaA. In the left and right subcomplexes, DnaA ATPases associated with various cellular activities (AAA+) domain III formed helices with specific structural differences in interdomain orientations, provoking a bend in the bound DNA. In the left subcomplex a continuous DnaA chain exists, including insertion of IHF into the DNA looping, consistent with the DNA unwinding function of the complex. The intervening spaces in those subcomplexes are crucial for DNA unwinding and loading of DnaB helicases. Taken together, this model provides a reasonable near-atomic level structural solution of the initiation complex, including the dynamic conformations and spatial arrangements of DnaA subcomplexes.
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