ArticleNature communications2025
Nucleosome unwrapping and PARP1 allostery drive affinities for chromatin and DNA breaks.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Structural basis of PARP2 recognition of nucleosomal DNA breaks and inhibitor trapping.Nucleic acids research · 2026Article
- Poly(ADP-Ribose) polymerase1 Has Potential to Facilitate the Nucleosome Disassembly.International journal of molecular sciences · 2026Article
- PARP1 Exhibits an Enzymatically Inactive Chromatin Binding Mode.bioRxiv : the preprint server for biology · 2026Article
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9 authors.
Funding
Abstract
Poly(ADP-ribose) polymerase 1 (PARP1) detects DNA strand breaks that occur in duplex DNA and chromatin. Here, correlative optical tweezers and fluorescence microscopy reveal how single molecules of PARP1 identify single-strand breaks (i.e., nicks), undamaged nucleosome core particles (NCP) and NCPs containing DNA nicks. Fluorescently-tagged PARP1 or PARP2 from nuclear extracts binds nicks with nanomolar affinity but does not engage undamaged dsDNA regions. In contrast, PARP1 avidly binds undamaged NCPs, and partial NCP unwrapping induced by DNA tension significantly increases PARP1 on rate and affinity. Catalytically dead PARP1 or EB-47 inhibition greatly increases PARP1 affinity to DNA nicks and undamaged NCP, implicating a mechanism where PARP1 reverse allostery regulates PARP1 retention to undamaged chromatin. We also monitor ADP-ribosylation in real time upon PARP1 binding undamaged or nicked NCPs. These results provide key mechanistic insights into domain allostery and how pharmacological intervention alters PARP1 binding dynamics for therapeutic impacts.
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Registered trials
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