ArticleMolecular cell2013
Nucleotide and partner-protein control of bacterial replicative helicase structure and function.
Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Cellular replisomes are powered by flex-fuel motors for unwinding DNA.Nature communications · 2026Article
- DNA translocation by the CMG helicase: the helical inchworm model.Biochemical Society transactions · 2026Review
- Dynamic DnaA-DnaB interactions at oriC coordinate the loading and coupled translocation of two DnaB helicases for bidirectional replication.Nucleic acids research · 2026Article
- 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
- 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
- Dysregulated DnaB unwinding induces replisome decoupling and daughter strand gaps that are countered by RecA polymerization.Nucleic acids research · 2024Article
- Escherichia coli DNA replication: the old model organism still holds many surprises.FEMS microbiology reviews · 2024Review
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- The Human Ocular Surface Microbiome and Its Associations with the Tear Proteome in Dry Eye Disease.International journal of molecular sciences · 2023Article
- 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
- Convergent evolution in two bacterial replicative helicase loaders.Trends in biochemical sciences · 2022Review
- Targeted chromosomal Escherichia coli:dnaB exterior surface residues regulate DNA helicase behavior to maintain genomic stability and organismal fitness.PLoS genetics · 2021Article
- Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase.Nature communications · 2021Article
- Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase.Nucleic acids research · 2021Article
- Paramagnetic Solid-State NMR to Localize the Metal-Ion Cofactor in an Oligomeric DnaB Helicase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Duplex DNA engagement and RPA oppositely regulate the DNA-unwinding rate of CMG helicase.Nature communications · 2020Article
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Authors and funding
7 authors.
Funding
Abstract
Cellular replication forks are powered by ring-shaped, hexameric helicases that encircle and unwind DNA. To better understand the molecular mechanisms and control of these enzymes, we used multiple methods to investigate the bacterial replicative helicase, DnaB. A 3.3 Å crystal structure of Aquifex aeolicus DnaB, complexed with nucleotide, reveals a newly discovered conformational state for this motor protein. Electron microscopy and small angle X-ray scattering studies confirm the state seen crystallographically, showing that the DnaB ATPase domains and an associated N-terminal collar transition between two physical states in a nucleotide-dependent manner. Mutant helicases locked in either collar state are active but display different capacities to support critical activities such as duplex translocation and primase-dependent RNA synthesis. Our findings establish the DnaB collar as an autoregulatory hub that controls the ability of the helicase to transition between different functional states in response to both nucleotide and replication initiation/elongation factors.
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