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DNA Polymerase Locks Replication Fork Under Stress

https://doi.org/10.1101/2024.10.09.617451
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1007/bf00928361openalex-snapshot
Physiological concentrations of purines and pyrimidines
inferredcites →https://doi.org/10.1016/j.bbapap.2009.06.012openalex-snapshot
DNA polymerase proofreading: Multiple roles maintain genome stability
inferredcites →https://doi.org/10.1016/j.bpj.2016.12.044openalex-snapshot
Switching between Exonucleolysis and Replication by T7 DNA Polymerase Ensures High Fidelity
inferredcites →https://doi.org/10.1016/j.cell.2017.11.017openalex-snapshot
Mfd Dynamically Regulates Transcription via a Release and Catch-Up Mechanism
inferredcites →https://doi.org/10.1016/j.celrep.2014.02.025openalex-snapshot
Helicase and Polymerase Move Together Close to the Fork Junction and Copy DNA in One-Nucleotide Steps
inferredcites →https://doi.org/10.1016/s0006-3495(02)75233-8openalex-snapshot
Probing Protein-DNA Interactions by Unzipping a Single DNA Double Helix
inferredcites →https://doi.org/10.1016/s0021-9258(17)44400-0openalex-snapshot
Two forms of the DNA polymerase of bacteriophage T7.
inferredcites →https://doi.org/10.1016/s0021-9258(17)44401-2openalex-snapshot
Characterization of strand displacement synthesis catalyzed by bacteriophage T7 DNA polymerase.
inferredcites →https://doi.org/10.1021/acsnano.8b03679openalex-snapshot
High-Performance Image-Based Measurements of Biological Forces and Interactions in a Dual Optical Trap
inferredcites →https://doi.org/10.1021/nl503009dopenalex-snapshot
DNA Y Structure: A Versatile, Multidimensional Single Molecule Assay
inferredcites →https://doi.org/10.1038/nature03615openalex-snapshot
DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase
inferredcites →https://doi.org/10.1038/nature10409openalex-snapshot
ATP-induced helicase slippage reveals highly coordinated subunits
inferredcites →https://doi.org/10.1038/ncomms10260openalex-snapshot
T7 replisome directly overcomes DNA damage
inferredcites →https://doi.org/10.1038/ncomms13337openalex-snapshot
DNA looping mediates nucleosome transfer
inferredcites →https://doi.org/10.1038/nrm.2016.88openalex-snapshot
Transcription–replication conflicts: how they occur and how they are resolved
inferredcites →https://doi.org/10.1038/nsmb.1526openalex-snapshot
High-resolution dynamic mapping of histone-DNA interactions in a nucleosome
inferredcites →https://doi.org/10.1038/nsmb.1798openalex-snapshot
Synergistic action of RNA polymerases in overcoming the nucleosomal barrier
inferredcites →https://doi.org/10.1038/nsmb1102openalex-snapshot
Probing SWI/SNF remodeling of the nucleosome by unzipping single DNA molecules
inferredcites →https://doi.org/10.1038/s41467-018-04702-xopenalex-snapshot
Helicase promotes replication re-initiation from an RNA transcript
inferredcites →https://doi.org/10.1038/s41589-022-01235-9openalex-snapshot
Etoposide promotes DNA loop trapping and barrier formation by topoisomerase II
inferredcites →https://doi.org/10.1038/s41594-022-00864-xopenalex-snapshot
Polarity of the CRISPR roadblock to transcription
inferredcites →https://doi.org/10.1038/s41598-019-49837-zopenalex-snapshot
Nuclease dead Cas9 is a programmable roadblock for DNA replication
inferredcites →https://doi.org/10.1073/pnas.0907147106openalex-snapshot
DNA polymerase ε and δ proofreading suppress discrete mutator and cancer phenotypes in mice
inferredcites →https://doi.org/10.1074/jbc.274.39.27481openalex-snapshot
Replication Slippage of Different DNA Polymerases Is Inversely Related to Their Strand Displacement Efficiency
inferredcites →https://doi.org/10.1074/jbc.m306893200openalex-snapshot
Unique Error Signature of the Four-subunit Yeast DNA Polymerase ϵ
inferredcites →https://doi.org/10.1083/jcb.201406100openalex-snapshot
DNA2 drives processing and restart of reversed replication forks in human cells
inferredcites →https://doi.org/10.1093/nar/gkaa1241openalex-snapshot
Catalytically inactive Cas9 impairs DNA replication fork progression to induce focal genomic instability
inferredcites →https://doi.org/10.1093/nar/gkad999openalex-snapshot
The proofreading exonuclease of leading-strand DNA polymerase epsilon prevents replication fork collapse at broken template strands
inferredcites →https://doi.org/10.1093/nar/gks253openalex-snapshot
Mechanism of strand displacement synthesis by DNA replicative polymerases
inferredcites →https://doi.org/10.1093/narcan/zcad005openalex-snapshot
Roles of trans-lesion synthesis (TLS) DNA polymerases in tumorigenesis and cancer therapy
inferredcites →https://doi.org/10.1103/physrevlett.91.028103openalex-snapshot
Dynamic Force Spectroscopy of Protein-DNA Interactions by Unzipping DNA
inferredcites →https://doi.org/10.1146/annurev.biochem.78.072407.103248openalex-snapshot
Motors, Switches, and Contacts in the Replisome
inferredcites →https://doi.org/10.15252/embj.2019103367openalex-snapshot
Excessive excision of correct nucleotides during DNA synthesis explained by replication hurdles
inferredcites →https://doi.org/10.7554/elife.06249openalex-snapshot
Dynamic regulation of transcription factors by nucleosome remodeling
inferredcites →https://doi.org/10.7554/elife.06562openalex-snapshot
Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1126/sciadv.adx4089openalex-snapshot
Real-time imaging of rotation during synthesis by the replisome
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