ArticleNucleic acids research2015
Structure and primase-mediated activation of a bacterial dodecameric replicative helicase.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- 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 basis of the T4 bacteriophage primosome assembly and primer synthesis.Nature communications · 2023Article
- Inhibition of Replication Fork Formation and Progression: Targeting the Replication Initiation and Primosomal Proteins.International journal of molecular sciences · 2023Review
- Structural basis of the T4 bacteriophage primosome assembly and primer synthesis.bioRxiv : the preprint server for biology · 2023Article
- Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase.Nature communications · 2021Article
- Biomolecular solid-state NMR spectroscopy at 1200 MHz: the gain in resolution.Journal of biomolecular NMR · 2021Article
- Article
- Nucleotide Binding Modes in a Motor Protein Revealed byChembiochem : a European journal of chemical biology · 2020Article
- Identification of the Unwinding Region in theFrontiers in microbiology · 2020Article
- Physical Basis for the Loading of a Bacterial Replicative Helicase onto DNA.Molecular cell · 2019Article
- The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase.Nature communications · 2019Article
- Article
- Segmental isotope labelling and solid-state NMR of a 12 × 59 kDa motor protein: identification of structural variability.Journal of biomolecular NMR · 2018Article
- Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.Journal of biomolecular NMR · 2017Article
- Review
- Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile.Open biology · 2016Article
- Variability and conservation of structural domains in divide-and-conquer approaches.Journal of biomolecular NMR · 2016Article
- 'Modulation of the enzymatic activities of replicative helicase (DnaB) by interaction with Hp0897: a possible mechanism for helicase loading in Helicobacter pylori'.Nucleic acids research · 2016Article
- Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.Journal of biomolecular NMR · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Replicative helicases are essential ATPases that unwind DNA to initiate chromosomal replication. While bacterial replicative DnaB helicases are hexameric, Helicobacter pylori DnaB (HpDnaB) was found to form double hexamers, similar to some archaeal and eukaryotic replicative helicases. Here we present a structural and functional analysis of HpDnaB protein during primosome formation. The crystal structure of the HpDnaB at 6.7 Å resolution reveals a dodecameric organization consisting of two hexamers assembled via their N-terminal rings in a stack-twisted mode. Using fluorescence anisotropy we show that HpDnaB dodecamer interacts with single-stranded DNA in the presence of ATP but has a low DNA unwinding activity. Multi-angle light scattering and small angle X-ray scattering demonstrate that interaction with the DnaG primase helicase-binding domain dissociates the helicase dodecamer into single ringed primosomes. Functional assays on the proteins and associated complexes indicate that these single ringed primosomes are the most active form of the helicase for ATP hydrolysis, DNA binding and unwinding. These findings shed light onto an activation mechanism of HpDnaB by the primase that might be relevant in other bacteria and possibly other organisms exploiting dodecameric helicases for DNA replication.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.