ArticleThe Journal of biological chemistry2013
The PriA replication restart protein blocks replicase access prior to helicase assembly and directs template specificity through its ATPase activity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 27 citations in OpenAlex.
- Visualization of the complete preprimosome reveals the structural mechanisms governing DNA replication restart.Nature communications · 2026Article
- Visualization of the complete primosome reveals the structural mechanisms governing DNA replication restart.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms of chromosomal DNA replication in Escherichia coli and Bacillus subtilis.FEMS microbiology reviews · 2026Review
- nCas9-based method for rolling-circle DNA substrate generation.Analytical biochemistry · 2025Article
- Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023Review
- Replication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli.Nature communications · 2023Article
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
- Identification of genetic interactions with priB links the PriA/PriB DNA replication restart pathway to double-strand DNA break repair in Escherichia coli.G3 (Bethesda, Md.) · 2022Article
- OB-fold Families of Genome Guardians: A Universal Theme Constructed From the Small β-barrel Building Block.Frontiers in molecular biosciences · 2022Review
- Escherichia coli K-12 has two distinguishable PriA-PriB replication restart pathways.Molecular microbiology · 2021Article
- Article
- Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.PloS one · 2021Article
- Genetic and metabolic signatures of Salmonella enterica subsp. enterica associated with animal sources at the pangenomic scale.BMC genomics · 2019Article
- Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Bacillus subtilis RarA modulates replication restart.Nucleic acids research · 2018Article
- Mechanisms of bacterial DNA replication restart.Nucleic acids research · 2018Review
- Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome.The Journal of biological chemistry · 2015Article
- A Replisome's journey through the bacterial chromosome.Frontiers in microbiology · 2015Review
- Bacillus subtilis RecA and its accessory factors, RecF, RecO, RecR and RecX, are required for spore resistance to DNA double-strand break.Nucleic acids research · 2014Article
- Structural mechanisms of PriA-mediated DNA replication restart.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The PriA protein serves as an initiator for the restart of DNA replication on stalled replication forks and as a checkpoint protein that prevents the replicase from advancing in a strand displacement reaction on forks that do not contain a functional replicative helicase. We have developed a primosomal protein-dependent fluorescence resonance energy transfer (FRET) assay using a minimal fork substrate composed of synthetic oligonucleotides. We demonstrate that a self-loading reaction, which proceeds at high helicase concentrations, occurs by threading of a preassembled helicase over free 5'-ends, an event that can be blocked by attaching a steric block to the 5'-end or coating DNA with single-stranded DNA binding protein. The specificity of PriA for replication forks is regulated by its intrinsic ATPase. ATPase-defective PriA K230R shows a strong preference for substrates that contain no gap between the leading strand and the duplex portion of the fork, as demonstrated previously. Wild-type PriA prefers substrates with larger gaps, showing maximal activity on substrates on which PriA K230R is inactive. We demonstrate that PriA blocks replicase function on forks by blocking its binding.
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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.