ArticleNature structural & molecular biology2022
Single-stranded nucleic acid binding and coacervation by linker histone H1.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 68 citations in OpenAlex.
- Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.Nature communications · 2026Article
- A Rahman Syndrome mutation in histone H1.4 disrupts chromatin compaction and phase separation.Nature communications · 2026Article
- Linker histone H1 functions as a liquid-like glue to organize chromatin in living human cells.Science advances · 2026Article
- Insights from single-molecule force spectroscopy into chromatin topology.Biophysical reviews · 2026Review
- Decoding nucleic acid contributions to phase separation and ordering in biomolecular condensates.Nucleic acids research · 2026Article
- Counteraction of HMGB1 at ss-dsDNA junctions maintains liquidity of protamine-DNA co-condensates.bioRxiv : the preprint server for biology · 2026Article
- Measuring bridging forces in protein-DNA condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Characterization of Non-Specific Electrostatic Interactions of Cationic Peptides with DNA Origami and Their Functional Consequences.Small methods · 2026Article
- Intrinsically disordered regions facilitate target search to drive promoter selectivity by a yeast transcription factor.Nature communications · 2025Article
- Protamine Drives Liquid and Solid Condensation of DNA and Glycosaminoglycans.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Liquid‒liquid phase separation: a potentially fundamental mechanism of sepsis.Cell death discovery · 2025Review
- Phase Separation in Chromatin Organization and Human Diseases.International journal of molecular sciences · 2025Review
- Toward Predictive Coarse-Grained Simulations of Biomolecular Condensates.Biochemistry · 2025Review
- Review
- Microphase separation produces interfacial environment within diblock biomolecular condensates.eLife · 2025Article
- Oligomerization-mediated phase separation in the nucleoid-associated sensory protein H-NS is controlled by ambient cues.Protein science : a publication of the Protein Society · 2025Article
- Shape transformations in peptide-DNA coacervates driven by enzyme-catalyzed deacetylation.Soft matter · 2024Article
- Protamine-Mediated Tangles Produce Extreme Deoxyribonucleic Acid Compaction.Journal of the American Chemical Society · 2024Article
- Differential dynamics specify MeCP2 function at nucleosomes and methylated DNA.Nature structural & molecular biology · 2024Article
- Super-resolution imaging reveals nucleolar encapsulation by single-stranded DNA.Journal of cell science · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 5 institutions in 1 country.
Funding
Abstract
The H1 linker histone family is the most abundant group of eukaryotic chromatin-binding proteins. However, their contribution to chromosome structure and function remains incompletely understood. Here we use single-molecule fluorescence and force microscopy to directly visualize the behavior of H1 on various nucleic acid and nucleosome substrates. We observe that H1 coalesces around single-stranded DNA generated from tension-induced DNA duplex melting. Using a droplet fusion assay controlled by optical tweezers, we find that single-stranded nucleic acids mediate the formation of gel-like H1 droplets, whereas H1-double-stranded DNA and H1-nucleosome droplets are more liquid-like. Molecular dynamics simulations reveal that multivalent and transient engagement of H1 with unpaired DNA strands drives their enhanced phase separation. Using eGFP-tagged H1, we demonstrate that inducing single-stranded DNA accumulation in cells causes an increase in H1 puncta that are able to fuse. We further show that H1 and Replication Protein A occupy separate nuclear regions, but that H1 colocalizes with the replication factor Proliferating Cell Nuclear Antigen, particularly after DNA damage. Overall, our results provide a refined perspective on the diverse roles of H1 in genome organization and maintenance, and indicate its involvement at stalled replication forks.
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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.