ArticleProceedings of the National Academy of Sciences of the United States of America2014
Single-molecule studies of polymerase dynamics and stoichiometry at the bacteriophage T7 replication machinery.
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 40 papers.
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Who cites it
40 citing papers in PubMed, 65 citations in OpenAlex.
- Real-time imaging of rotation during synthesis by the replisome.Science advances · 2026Article
- Structural insights into the exchange mechanism of a replicative DNA polymerase.Nucleic acids research · 2025Article
- nCas9-based method for rolling-circle DNA substrate generation.Analytical biochemistry · 2025Article
- Insight into Single-Molecule Imaging Techniques for the Study of Prokaryotic Genome Maintenance.Chemical & biomedical imaging · 2024Review
- Mapping fast DNA polymerase exchange during replication.Nature communications · 2024Article
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- Single-molecule visualization of stalled replication-fork rescue by the Escherichia coli Rep helicase.Nucleic acids research · 2023Article
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
- Computationally exploring the mechanism of bacteriophage T7 gp4 helicase translocating along ssDNA.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural and Molecular Kinetic Features of Activities of DNA Polymerases.International journal of molecular sciences · 2022Review
- Bayesian machine learning analysis of single-molecule fluorescence colocalization images.eLife · 2022Article
- Observing protein dynamics during DNA-lesion bypass by the replisome.Frontiers in molecular biosciences · 2022Review
- DnaB helicase dynamics in bacterial DNA replication resolved by single-molecule studies.Nucleic acids research · 2021Article
- Single-Molecule Fluorescence Methods to Study Protein Exchange Kinetics in Supramolecular Complexes.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Single-Molecule Insights Into the Dynamics of Replicative Helicases.Frontiers in molecular biosciences · 2021Review
- DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021Review
- DNA polymerase stalling at structured DNA constrains the expansion of short tandem repeats.Genome biology · 2020Article
- A Primase-Induced Conformational Switch Controls the Stability of the Bacterial Replisome.Molecular cell · 2020Article
- Caught in the act: structural dynamics of replication origin activation and fork progression.Biochemical Society transactions · 2020Review
- Biphasic unbinding of a metalloregulator from DNA for transcription (de)repression in Live Bacteria.Nucleic acids research · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Replication of DNA plays a central role in transmitting hereditary information from cell to cell. To achieve reliable DNA replication, multiple proteins form a stable complex, known as the replisome, enabling them to act together in a highly coordinated fashion. Over the past decade, the roles of the various proteins within the replisome have been determined. Although many of their interactions have been characterized, it remains poorly understood how replication proteins enter and leave the replisome. In this study, we visualize fluorescently labeled bacteriophage T7 DNA polymerases within the replisome while we simultaneously observe the kinetics of the replication process. This combination of observables allows us to monitor both the activity and dynamics of individual polymerases during coordinated leading- and lagging-strand synthesis. Our data suggest that lagging-strand polymerases are exchanged at a frequency similar to that of Okazaki fragment synthesis and that two or more polymerases are present in the replisome during DNA replication. Our studies imply a highly dynamic picture of the replisome with lagging-strand DNA polymerases residing at the fork for the synthesis of only a few Okazaki fragments. Further, new lagging-strand polymerases are readily recruited from a pool of polymerases that are proximally bound to the replisome and continuously replenished from solution.
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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.