ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural mechanisms of PriA-mediated DNA replication restart.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed, 108 citations in OpenAlex.
- Nanoscale Analysis of SSB-RecO Interplay in SSB Interaction with the Target.International journal of molecular sciences · 2026Article
- Domain dynamics within the PriA DNA helicase regulate DNA replication restart.Nucleic acids research · 2026Article
- A superfamily 1 helicase translocates on double-stranded DNA.bioRxiv : the preprint server for biology · 2026Article
- 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
- Novel mutations in the RECQL4 gene affect its helicase functions, interactions with the BLM helicase and chemotherapeutics-induced cell death.Cell death discovery · 2025Article
- Protein-Protein Interactions as Promising Molecular Targets for Novel Antimicrobials Aimed at Gram-Negative Bacteria.International journal of molecular sciences · 2025Review
- DNA polymerase actively and sequentially displaces single-stranded DNA-binding proteins.Nature communications · 2025Article
- The YoaA-χ helicase modulates the dynamics of single-stranded DNA binding protein on DNA.Nature communications · 2025Article
- Article
- Single-stranded DNA binding protein hitches a ride with thebioRxiv : the preprint server for biology · 2024Article
- The mutation R107Q alters mtSSB ssDNA compaction ability and binding dynamics.Nucleic acids research · 2024Article
- The intrinsically disordered linker in the single-stranded DNA-binding protein influences DNA replication restart and recombination pathways inJournal of bacteriology · 2024Article
- Hachiman is a genome integrity sensor.bioRxiv : the preprint server for biology · 2024Article
- Regulation of T7 gp2.5 binding dynamics by its C-terminal tail, template conformation and sequence.Nucleic acids research · 2023Article
- Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023Review
- RecF protein targeting to postreplication (daughter strand) gaps I: DNA binding by RecF and RecFR.Nucleic acids research · 2023Article
- Replication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli.Nature communications · 2023Article
- Interaction with the carboxy-terminal tip of SSB is critical for RecG function in E. coli.Nucleic acids research · 2023Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Collisions between cellular DNA replication machinery (replisomes) and damaged DNA or immovable protein complexes can dissociate replisomes before the completion of replication. This potentially lethal problem is resolved by cellular "replication restart" reactions that recognize the structures of prematurely abandoned replication forks and mediate replisomal reloading. In bacteria, this essential activity is orchestrated by the PriA DNA helicase, which identifies replication forks via structure-specific DNA binding and interactions with fork-associated ssDNA-binding proteins (SSBs). However, the mechanisms by which PriA binds replication fork DNA and coordinates subsequent replication restart reactions have remained unclear due to the dearth of high-resolution structural information available for the protein. Here, we describe the crystal structures of full-length PriA and PriA bound to SSB. The structures reveal a modular arrangement for PriA in which several DNA-binding domains surround its helicase core in a manner that appears to be poised for binding to branched replication fork DNA structures while simultaneously allowing complex formation with SSB. PriA interaction with SSB is shown to modulate SSB/DNA complexes in a manner that exposes a potential replication initiation site. From these observations, a model emerges to explain how PriA links recognition of diverse replication forks to replication restart.
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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.