ArticleNature communications2024
Mapping fast DNA polymerase exchange during replication.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Concurrent positional dynamics and activity mapping of DNA-binding proteins.Nature protocols · 2026Review
- Real-time electrical monitoring of enzymatic catalytic dynamics at the single-molecule level.Nature communications · 2026Article
- Multiple strategies to resolve the conflict between replication and transcription in mammalian cells.Nucleic acids research · 2026Article
- DNA polymerase actively and sequentially displaces single-stranded DNA-binding proteins.Nature communications · 2025Article
- The proofreading mechanism of the human leading-strand DNA polymerase ε holoenzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Tunable elliptical cylinders for rotational mechanical studies of single DNA molecules.Science advances · 2024Article
- Tunable Elliptical Cylinders for Rotational Mechanical Studies of Single DNA Molecules.bioRxiv : the preprint server for biology · 2024Article
- Mapping fast DNA polymerase exchange during replication.Nature communications · 2024Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
Despite extensive studies on DNA replication, the exchange mechanisms of DNA polymerase during replication remain unclear. Existing models propose that this exchange is facilitated by protein partners like helicase. Here we present data, employing a combination of mechanical DNA manipulation and single fluorescent protein observation, that reveal DNA polymerase undergoing rapid and autonomous exchange during replication not coordinated by other proteins. The DNA polymerase shows fast unbinding and rebinding dynamics, displaying a preference for either exonuclease or polymerase activity, or pausing events, during each brief binding event. We also observed a 'memory effect' in DNA polymerase rebinding, i.e., the enzyme tends to preserve its prior activity upon reassociation. This effect, potentially linked to the ssDNA/dsDNA junction's conformation, might play a role in regulating binding preference enabling high processivity amidst rapid protein exchange. Taken together, our findings support an autonomous replication model that includes rapid protein exchange, burst of activity, and a 'memory effect' while moving processively forward.
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