ArticleNucleic acids research2009
A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 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
- DnaB and DciA: mechanisms of helicase loading and translocation on ssDNA.Nucleic acids research · 2025Article
- 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
- 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
- Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly.Nature communications · 2013Article
- Mechanisms for initiating cellular DNA replication.Annual review of biochemistry · 2013Review
- Loading mechanisms of ring helicases at replication origins.Molecular microbiology · 2012Review
- Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Current drug targets · 2012Review
- Glutarate and N-acetyl-L-glutamate buffers for cell-free synthesis of selectively 15N-labelled proteins.Journal of biomolecular NMR · 2009Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The helicase loader protein DnaI (the Bacillus subtilis homologue of Escherichia coli DnaC) is required to load the hexameric helicase DnaC (the B. subtilis homologue of E. coli DnaB) onto DNA at the start of replication. While the C-terminal domain of DnaI belongs to the structurally well-characterized AAA+ family of ATPases, the structure of the N-terminal domain, DnaI-N, has no homology to a known structure. Three-dimensional structure determination by nuclear magnetic resonance (NMR) spectroscopy shows that DnaI presents a novel fold containing a structurally important zinc ion. Surface plasmon resonance experiments indicate that DnaI-N is largely responsible for binding of DnaI to the hexameric helicase from B. stearothermophilus, which is a close homologue of the corresponding much less stable B. subtilis helicase.
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