ArticleNucleic acids research2021
Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase.
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 13 papers.
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13 citing papers in PubMed, 28 citations in OpenAlex.
- Distinct quaternary states, intermediates, and autoinhibition during loading of the DnaB-replicative helicase by the phage λP helicase loader.Nucleic acids research · 2025Article
- DnaB and DciA: mechanisms of helicase loading and translocation on ssDNA.Nucleic acids research · 2025Article
- DciA secures bidirectional replication initiation in Vibrio cholerae.Nucleic acids research · 2024Article
- Frequent nonhomologous replacement of replicative helicase loaders by viruses inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cell cycle-coordinated maintenance of theEcoSal Plus · 2023Review
- Inhibition of Replication Fork Formation and Progression: Targeting the Replication Initiation and Primosomal Proteins.International journal of molecular sciences · 2023Review
- Diverse Mechanisms of Helicase Loading during DNA Replication Initiation in Bacteria.Journal of bacteriology · 2023Review
- The LH-DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders.Acta crystallographica. Section D, Structural biology · 2023Article
- Structural Insights of the DciA Helicase Loader in Its Relationship with DNA.International journal of molecular sciences · 2023Article
- The Caulobacter crescentus DciA promotes chromosome replication through topological loading of the DnaB replicative helicase at replication forks.Nucleic acids research · 2022Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- DciA Helicase Operators Exhibit Diversity across Bacterial Phyla.Journal of bacteriology · 2022Article
- Convergent evolution in two bacterial replicative helicase loaders.Trends in biochemical sciences · 2022Review
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Authors and funding
17 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Replicative helicases are essential proteins that unwind DNA in front of replication forks. Their loading depends on accessory proteins and in bacteria, DnaC and DnaI are well characterized loaders. However, most bacteria do not express either of these two proteins. Instead, they are proposed to rely on DciA, an ancestral protein unrelated to DnaC/I. While the DciA structure from Vibrio cholerae shares no homology with DnaC, it reveals similarities with DnaA and DnaX, two proteins involved during replication initiation. As other bacterial replicative helicases, VcDnaB adopts a toroid-shaped homo-hexameric structure, but with a slightly open dynamic conformation in the free state. We show that VcDnaB can load itself on DNA in vitro and that VcDciA stimulates this function, resulting in an increased DNA unwinding. VcDciA interacts with VcDnaB with a 3/6 stoichiometry and we show that a determinant residue, which discriminates DciA- and DnaC/I-helicases, is critical in vivo. Our work is the first step toward the understanding of the ancestral mode of loading of bacterial replicative helicases on DNA. It sheds light on the strategy employed by phage helicase loaders to hijack bacterial replicative helicases and may explain the recurrent domestication of dnaC/I through evolution in bacteria.
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