ArticleMolecular cell2010
Primase directs the release of DnaC from DnaB.
Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
56 citing papers in PubMed, 87 citations in OpenAlex.
- Cellular replisomes are powered by flex-fuel motors for unwinding DNA.Nature communications · 2026Article
- Dynamic DnaA-DnaB interactions at oriC coordinate the loading and coupled translocation of two DnaB helicases for bidirectional replication.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
- Diverse Mechanisms of Helicase Loading during DNA Replication Initiation in Bacteria.Journal of bacteriology · 2023Review
- The Caulobacter crescentus DciA promotes chromosome replication through topological loading of the DnaB replicative helicase at replication forks.Nucleic acids research · 2022Article
- Convergent evolution in two bacterial replicative helicase loaders.Trends in biochemical sciences · 2022Review
- Concerted actions of DnaA complexes with DNA-unwinding sequences within and flanking replication origin oriC promote DnaB helicase loading.The Journal of biological chemistry · 2022Article
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- DnaB helicase dynamics in bacterial DNA replication resolved by single-molecule studies.Nucleic acids research · 2021Article
- The molecular coupling between substrate recognition and ATP turnover in a AAA+ hexameric helicase loader.eLife · 2021Article
- DnaB helicase is recruited to the replication initiation complex via binding of DnaA domain I to the lateral surface of the DnaB N-terminal domain.The Journal of biological chemistry · 2020Article
- Metabolic cofactors NADH and FAD act as non-canonical initiating substrates for a primase and affect replication primer processing in vitro.Nucleic acids research · 2020Article
- Bacillus subtilis RecA interacts with and loads RadA/Sms to unwind recombination intermediates during natural chromosomal transformation.Nucleic acids research · 2019Article
- Physical Basis for the Loading of a Bacterial Replicative Helicase onto DNA.Molecular cell · 2019Article
- Article
- Mycobacterial DnaB helicase intein as oxidative stress sensor.Nature communications · 2018Article
- The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.Antibiotics (Basel, Switzerland) · 2018Review
- The DnaA AAA+ Domain His136 Residue Directs DnaB Replicative Helicase to the Unwound Region of the Replication Origin,Frontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
An AAA+ ATPase, DnaC, delivers DnaB helicase at the E. coli chromosomal origin by a poorly understood process. This report shows that mutant proteins bearing alanine substitutions for two conserved arginines in a motif named box VII are defective in DNA replication, but this deficiency does not arise from impaired interactions with ATP, DnaB, or single-stranded DNA. Despite their ability to deliver DnaB to the chromosomal origin to form the prepriming complex, this intermediate is inactive. Quantitative analysis of the prepriming complex suggests that the DnaB-DnaC complex contains three DnaC monomers per DnaB hexamer and that the interaction of primase with DnaB and primer formation triggers the release of DnaC, but not the mutants, from DnaB. The interaction of primase with DnaB and the release of DnaC mark discrete events in the transition from initiation to the elongation stage of DNA replication.
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What OpenQuestion holds
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.