ArticleActa crystallographica. Section D, Structural biology2023
The LH-DH module of bacterial replicative helicases is the common binding site for DciA and other helicase loaders.
Article in Acta crystallographica. Section D, Structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 10 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
- Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.Science advances · 2024Article
- Structural Insights of the DciA Helicase Loader in Its Relationship with DNA.International journal of molecular sciences · 2023Article
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Authors and funding
8 authors at 2 institutions in 1 country.
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Abstract
During the initiation step of bacterial genome replication, replicative helicases depend on specialized proteins for their loading onto oriC. DnaC and DnaI were the first loaders to be characterized. However, most bacteria do not contain any of these genes, which are domesticated phage elements that have replaced the ancestral and unrelated loader gene dciA several times during evolution. To understand how DciA assists the loading of DnaB, the crystal structure of the complex from Vibrio cholerae was determined, in which two VcDciA molecules interact with a dimer of VcDnaB without changing its canonical structure. The data showed that the VcDciA binding site on VcDnaB is the conserved module formed by the linker helix LH of one monomer and the determinant helix DH of the second monomer. Interestingly, DnaC from Escherichia coli also targets this module onto EcDnaB. Thanks to their common target site, it was shown that VcDciA and EcDnaC could be functionally interchanged in vitro despite sharing no structural similarity. This represents a milestone in understanding the mechanism employed by phage helicase loaders to hijack bacterial replicative helicases during evolution.
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