ArticleNature communications2013
Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Bacillus subtilis DnaB forms multiple protein-protein interactions essential for DNA replication initiation.Nucleic acids research · 2026Article
- Mechanisms of chromosomal DNA replication in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2026Review
- 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
- Article
- Structural basis of the T4 bacteriophage primosome assembly and primer synthesis.Nature communications · 2023Article
- Structural basis of the T4 bacteriophage primosome assembly and primer synthesis.bioRxiv : the preprint server for biology · 2023Article
- 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
- The Caulobacter crescentus DciA promotes chromosome replication through topological loading of the DnaB replicative helicase at replication forks.Nucleic acids research · 2022Article
- DciA Helicase Operators Exhibit Diversity across Bacterial Phyla.Journal of bacteriology · 2022Article
- Article
- Physical Basis for the Loading of a Bacterial Replicative Helicase onto DNA.Molecular cell · 2019Article
- Cryptic protein interactions regulate DNA replication initiation.Molecular microbiology · 2019Article
- Article
- Multiple links connect central carbon metabolism to DNA replication initiation and elongation in Bacillus subtilis.DNA research : an international journal for rapid publication of reports on genes and genomes · 2018Article
- The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.Antibiotics (Basel, Switzerland) · 2018Review
- Bacterial DnaB helicase interacts with the excluded strand to regulate unwinding.The Journal of biological chemistry · 2017Article
- Review
- Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile.Open biology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC DNA and then dissociate from the complex. Here, to provide a better understanding of this key process, we report the crystal structure of the ~570-kDa prepriming complex between the Bacillus subtilis loader protein and the Bacillus stearothermophilus helicase, as well as the helicase-binding domain of primase with a molar ratio of 6:6:3 at 7.5 Å resolution. The overall architecture of the complex exhibits a three-layered ring conformation. Moreover, the structure combined with the proposed model suggests that the shift from the 'open-ring' to the 'open-spiral' and then the 'closed-spiral' state of the helicase ring due to the binding of single-stranded DNA may be the cause of the loader release.
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Registered trials
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.