ArticleNature communications2026
Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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1 citing paper in PubMed.
- Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.Nature communications · 2026Article
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3 authors.
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Abstract
In the sperm nucleus, protamine replaces histones to mediate extreme DNA compaction. The histone-to-protamine transition involves the occurrence of double-strand breaks, and is facilitated by transition proteins including those containing high-mobility-group boxes. Here we use optical tweezers and microscopy to study the actions of HMGB1 and protamine on DNA. Confocal scans of GFP-HMGB1 on overstretched λ-DNA show 2-3 foci that spread on the DNA upon retraction. Spreading of foci coincides with reannealing of ssDNA tracts, confirming their localization at ss-dsDNA junctions. Whereas the force-extension curves of protamine-soaked λ-DNA show tangles that withstand forces > 60 pN, premixing protamine with HMGB1 produces only bends and bridges ( ~ 20 pN). The counteraction of HMGB1 involves its acidic C-terminal tail, as HMGB1-ΔC fails to prevent tangle formation. In line with these single-molecule results, brightfield and confocal imaging show that protamine-dsDNA aggregates change to liquid droplets in the presence of HMGB1 but not HMGB1-ΔC. Similar to HMGB1, human transition protein 1 counteracts the effects of protamine on DNA condensation. p53, a recruiter of repair factors, colocalizes with HMGB1 and protamine at ss-dsDNA junctions. Together, these observations support our hypothesis that chromatin-associated proteins like HMGB1 help maintain early protamine-mediated DNA condensates in a liquid state to facilitate the repair of double-strand breaks.
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