ArticleNucleic acids research2013
Insights into the structure and assembly of the Bacillus subtilis clamp-loader complex and its interaction with the replicative helicase.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Single-molecule tracking of RNA-DNA hybrid removal enzymes important for lagging-strand replication.Biophysical journal · 2026Article
- DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026Review
- Mechanisms of chromosomal DNA replication in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2026Review
- Single-molecule tracking of RNA-DNA hybrid removal enzymes important for lagging-strand replication.bioRxiv : the preprint server for biology · 2025Article
- Replisomal coupling between the α-pol III core and the τ-subunit of the clamp loader complex (CLC) are essential for genomic integrity in Escherichia coli.The Journal of biological chemistry · 2025Article
- Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry.Journal of visualized experiments : JoVE · 2018Article
- Bacillus subtilis RarA modulates replication restart.Nucleic acids research · 2018Article
- Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex.Nucleic acids research · 2017Article
- Interactions of theOpen biology · 2017Article
- Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile.Open biology · 2016Article
- Nucleotide and partner-protein control of bacterial replicative helicase structure and function.Molecular cell · 2013Article
- Crystal structure and mode of helicase binding of the C-terminal domain of primase from Helicobacter pylori.Journal of bacteriology · 2013Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
The clamp-loader complex plays a crucial role in DNA replication by loading the β-clamp onto primed DNA to be used by the replicative polymerase. Relatively little is known about the stoichiometry, structure and assembly pathway of this complex, and how it interacts with the replicative helicase, in Gram-positive organisms. Analysis of full and partial complexes by mass spectrometry revealed that a hetero-pentameric τ3-δ-δ' Bacillus subtilis clamp-loader assembles via multiple pathways, which differ from those exhibited by the Gram-negative model Escherichia coli. Based on this information, a homology model of the B. subtilis τ3-δ-δ' complex was constructed, which revealed the spatial positioning of the full C-terminal τ domain. The structure of the δ subunit was determined by X-ray crystallography and shown to differ from that of E. coli in the nature of the amino acids comprising the τ and δ' binding regions. Most notably, the τ-δ interaction appears to be hydrophilic in nature compared with the hydrophobic interaction in E. coli. Finally, the interaction between τ3 and the replicative helicase DnaB was driven by ATP/Mg(2+) conformational changes in DnaB, and evidence is provided that hydrolysis of one ATP molecule by the DnaB hexamer is sufficient to stabilize its interaction with τ3.
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