ArticleGenes to cells : devoted to molecular & cellular mechanisms2016
SSB binds to the RecG and PriA helicases in vivo in the absence of DNA.
Article in Genes to cells : devoted to molecular & cellular mechanisms, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 45 citations in OpenAlex.
- A novel ψ-χ fusion protein for unravelling the contributions of χ to DNA replication and repair.Nucleic acids research · 2026Article
- A NovelbioRxiv : the preprint server for biology · 2026Article
- Anti-Skin Aging Potential, Antibacterial Activity, Inhibition of Single-Stranded DNA-Binding Protein, and Cytotoxic Effects of Acetone-ExtractedPlants (Basel, Switzerland) · 2024Article
- Allosteric effects of E. coli SSB and RecR proteins on RecO protein binding to DNA.Nucleic acids research · 2023Article
- Replication stalling activates SSB for recruitment of DNA damage tolerance factors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Biochemical Mechanism of Fork Regression in Prokaryotes and Eukaryotes-A Single Molecule Comparison.International journal of molecular sciences · 2022Review
- How Glutamate Promotes Liquid-liquid Phase Separation and DNA Binding Cooperativity of E. coli SSB Protein.Journal of molecular biology · 2022Article
- OB-fold Families of Genome Guardians: A Universal Theme Constructed From the Small β-barrel Building Block.Frontiers in molecular biosciences · 2022Review
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- Characterization of the Chimeric PriB-SSBc Protein.International journal of molecular sciences · 2021Article
- The mechanism of action of the SSB interactome reveals it is the first OB-fold family of genome guardians in prokaryotes.Protein science : a publication of the Protein Society · 2021Review
- Article
- Single-molecule insight into stalled replication fork rescue in Escherichia coli.Nucleic acids research · 2021Review
- Dynamics of the PriA Helicase at Stalled DNA Replication Forks.The journal of physical chemistry. B · 2021Article
- Characterize the Interaction of the DNA Helicase PriA with the Stalled DNA Replication Fork Using Atomic Force Microscopy.Bio-protocol · 2021Article
- Allosteric effects of SSB C-terminal tail on assembly of E. coli RecOR proteins.Nucleic acids research · 2021Article
- In Vivo Binding of Single-Stranded DNA-Binding Protein to Stalled Replication Fork Helicases.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Phase separation by ssDNA binding protein controlled via protein-protein and protein-DNA interactions.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Atomic force microscopy-based characterization of the interaction of PriA helicase with stalled DNA replication forks.The Journal of biological chemistry · 2020Article
- The mechanism of Single strand binding protein-RecG binding: Implications for SSB interactome function.Protein science : a publication of the Protein Society · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The E. coli single-stranded DNA-binding protein (SSB) binds to the fork DNA helicases RecG and PriA in vitro. Typically for binding to occur, 1.3 m ammonium sulfate must be present, bringing into question the validity of these results as these are nonphysiological conditions. To determine whether SSB can bind to these helicases, we examined binding in vivo. First, using fluorescence microscopy, we show that SSB localizes PriA and RecG to the vicinity of the inner membrane in the absence of DNA damage. Localization requires that SSB be in excess over the DNA helicases and the SSB C-terminus and both PriA and RecG be present. Second, using the purification of tagged complexes, our results show that SSB binds to PriA and RecG in vivo, in the absence of DNA. We propose that this may be the 'storage form' of RecG and PriA. We further propose that when forks stall, RecG and PriA are targeted to the fork by SSB, which, by virtue of its high affinity for single-stranded DNA, allows these helicases to outcompete other proteins. This ensures their actions in the early stages of the rescue of stalled replication forks.
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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.