ArticleNucleic acids research2016
Stability versus exchange: a paradox in DNA replication.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Real-time imaging of rotation during synthesis by the replisome.Science advances · 2026Article
- Article
- Mapping fast DNA polymerase exchange during replication.Nature communications · 2024Article
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- Facilitated dissociation of nucleoid-associated proteins from DNA in the bacterial confinement.Biophysical journal · 2022Article
- Multiple roles of Pol epsilon in eukaryotic chromosome replication.Biochemical Society transactions · 2022Article
- Dynamics of Proteins and Macromolecular Machines in Escherichia coli.EcoSal Plus · 2021Review
- Single-Molecule Fluorescence Methods to Study Protein Exchange Kinetics in Supramolecular Complexes.Methods in molecular biology (Clifton, N.J.) · 2021Article
- DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021Review
- Caught in the act: structural dynamics of replication origin activation and fork progression.Biochemical Society transactions · 2020Review
- Article
- Tunability of DNA Polymerase Stability during Eukaryotic DNA Replication.Molecular cell · 2020Article
- How do DNA-bound proteins leave their binding sites? The role of facilitated dissociation.Current opinion in chemical biology · 2019Review
- Force-Dependent Facilitated Dissociation Can Generate Protein-DNA Catch Bonds.Biophysical journal · 2019Article
- When proteins play tag: the dynamic nature of the replisome.Biophysical reviews · 2019Review
- Recycling of single-stranded DNA-binding protein by the bacterial replisome.Nucleic acids research · 2019Article
- Polarized displacement by transcription activator-like effectors for regulatory circuits.Nature chemical biology · 2019Article
- Facilitated Unbinding via Multivalency-Enabled Ternary Complexes: New Paradigm for Protein-DNA Interactions.Accounts of chemical research · 2018Review
- A change of view: homologous recombination at single-molecule resolution.Nature reviews. Genetics · 2018Review
- Effects of electrostatic interactions on ligand dissociation kinetics.Physical review. E · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multi-component biological machines, comprising individual proteins with specialized functions, perform a variety of essential processes in cells. Once assembled, most such complexes are considered very stable, retaining individual constituents as long as required. However, rapid and frequent exchange of individual factors in a range of critical cellular assemblies, including DNA replication machineries, DNA transcription regulators and flagellar motors, has recently been observed. The high stability of a multi-protein complex may appear mutually exclusive with rapid subunit exchange. Here, we describe a multisite competitive exchange mechanism, based on simultaneous binding of a protein to multiple low-affinity sites. It explains how a component can be stably integrated into a complex in the absence of competing factors, while able to rapidly exchange in the presence of competing proteins. We provide a mathematical model for the mechanism and give analytical expressions for the stability of a pre-formed complex, in the absence and presence of competitors. Using typical binding kinetic parameters, we show that the mechanism is operational under physically realistic conditions. Thus, high stability and rapid exchange within a complex can be reconciled and this framework can be used to rationalize previous observations, qualitatively as well as quantitatively.
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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.