ArticleBiophysical journal2020
Liquid-Liquid Phase Separation of Histone Proteins in Cells: Role in Chromatin Organization.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 156 citations in OpenAlex.
- Mixing chromatin fibers with different nucleosome repeat lengths changes dynamics of chromatin phase separation.The Journal of biological chemistry · 2026Article
- From chromosomal protein disorder to chromatin phase separation.Epigenetics & chromatin · 2026Review
- Supercoils Stabilize a "DNA Corset" Condensate with Torsion-Dependent Hysteretic Compaction.JACS Au · 2026Article
- Revealing site-specific molecular features mediating contacts of heterochromatin protein 1 α (HP1α) and the interactions with chromatin and DNA in LLPS environments.Communications biology · 2025Article
- Multiscale structure of chromatin condensates explains phase separation and material properties.Science (New York, N.Y.) · 2025Article
- Tau Liquid-Liquid Phase Separation in Alzheimer's Disease: Mechanisms, Pathogenesis, and Therapeutic Implications.Molecular neurobiology · 2025Review
- Liquid-Liquid Phase Separation: Mechanisms, Roles, and Implications in Cellular Function and Disease.FASEB bioAdvances · 2025Review
- Expanding the HP1a-binding consensus and molecular grammar for heterochromatin assembly.Nucleic acids research · 2025Article
- Article
- Chiral Matching between Nucleic Acids and Polypeptides Facilitates Liquid-Liquid Phase Separation.The journal of physical chemistry letters · 2025Article
- Peptide Coacervates Can Protect Sequestered Oligonucleotides from Nucleases and Release Them for Transcription and Translation.Biomacromolecules · 2025Article
- Peripheral heterochromatin tethering is required for chromatin-based nuclear mechanical response.Nucleic acids research · 2025Article
- Phase Separation in Chromatin Organization and Human Diseases.International journal of molecular sciences · 2025Review
- Intrinsic Disorder and Phase Separation Coordinate Exocytosis, Motility, and Chromatin Remodeling in the Human Acrosomal Proteome.Proteomes · 2025Article
- Chemically Informed Coarse-Graining of Electrostatic Forces in Charge-Rich Biomolecular Condensates.ACS central science · 2025Article
- Insights on the effect of macromolecular crowding on transcription and its regulation.QRB discovery · 2025Article
- Liquid-liquid phase separation in cell physiology and cancer biology: recent advances and therapeutic implications.Frontiers in oncology · 2025Review
- Unveiling structural and dynamical features of chromatin using NMR spectroscopy.Magnetic resonance letters · 2024Review
- Emerging roles of liquid-liquid phase separation in liver innate immunity.Cell communication and signaling : CCS · 2024Review
- Chromosome compartmentalization: causes, changes, consequences, and conundrums.Trends in cell biology · 2024Review
24 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Liquid-liquid phase separation (LLPS) of proteins and nucleic acids has emerged as an important phenomenon in membraneless intracellular organization. We demonstrate that the linker histone H1 condenses into liquid-like droplets in the nuclei of HeLa cells. The droplets, observed during the interphase of the cell cycle, are colocalized with DNA-dense regions indicative of heterochromatin. In vitro, H1 readily undergoes LLPS with both DNA and nucleosomes of varying lengths but does not phase separate in the absence of DNA. The nucleosome core particle maintains its structural integrity inside the droplets, as demonstrated by FRET. Unexpectedly, H2A also forms droplets in the presence of DNA and nucleosomes in vitro, whereas the other core histones precipitate. The phase diagram of H1 with nucleosomes is invariant to the nucleosome length at physiological salt concentration, indicating that H1 is capable of partitioning large segments of DNA into liquid-like droplets. Of the proteins tested (H1, core histones, and the heterochromatin protein HP1α), this property is unique to H1. In addition, free nucleotides promote droplet formation of H1 nucleosome in a nucleotide-dependent manner, with droplet formation being most favorable with ATP. Although LLPS of HP1α is known to contribute to the organization of heterochromatin, our results indicate that H1 also plays a role. Based on our study, we propose that H1 and DNA act as scaffolds for phase-separated heterochromatin domains.
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