HP1a promotes chromatin liquidity and drives spontaneous heterochromatin compartmentalization
Lucy D. BrennaniD, Hyeong-Ku Kim, Serafin U. ColmenaresiD, Tatum Ego, Je‐Kyung RyuiD, Gary H. KarpeniD
Abstract
Compartmentalization of the nucleus into heterochromatin and euchromatin is highly conserved across eukaryotes. Constitutive heterochromatin (C-Het) constitutes a liquid-like condensate that packages the repetitive regions of the genome through the enrichment of histone modification H3K9me3 and recruitment of its cognate reader protein Heterochromatin Protein-1 (HP1a). The ability for well-ordered nucleosome arrays and HP1a to independently form biomolecular condensates suggests that the emergent material properties of C-Het compartments may contribute to its functions such as force-buffering, dosage-dependent gene silencing, and selective permeability. Using an in vitro reconstitution system we directly assess the contributions of H3K9me3 and HP1a on the biophysical properties of C-Het. In the presence of HP1a, H3K9me3 (Me-) and unmodified (U-) chromatin form co-condensates composed of distinct, immiscible domains. These chromatin domains form spontaneously and are reversible. Independently of HP1a, H3K9me3 modifications are sufficient to increase linker-DNA length within chromatin arrays and slow chromatin condensate growth. HP1a increases the liquidity of chromatin condensates while dramatically differentiating the viscoelastic properties of Me-chromatin versus U-chromatin. Mutating key residues in HP1a show that HP1a interactions with itself and chromatin determine the relative interfacial tension between chromatin compartments, however the formation of condensates is driven by the underlying chromatin. These direct measurements map the energetic landscape that determines C-Het compartmentalization, demonstrating that nuclear compartmentalization is a spontaneous and energetically favorable process in which HP1a plays a critical role in establishing a hierarchy of affinities between H3K9me3-chromatin and unmodified-chromatin. Highlights HP1a is necessary and sufficient for heterochromatin compartmentalization. Heterochromatin compartmentalization is reversible and proceeds through microphase-separation. H3K9me3 is sufficient to change nucleosome-array dynamics and mesoscale material properties. HP1a increases chromatin liquidity. HP1a-chromatin interaction modes tune the interfacial tensions and morphologies of heterochromatin compartments.
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 13
- FWCI
- 10.30
- Field percentile
- top 1%
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- HP1-driven phase separation recapitulates the thermodynamics and kinetics of heterochromatin condensate formation
M. M. Tortora, L. Brennan, … D. Jost·bioRxiv·Jul 11, 2022
- Modified histone peptides uniquely tune the material properties of HP1α condensates.
Priyasha Deshpande, Emily Prentice, … Shana Elbaum‐Garfinkle·Biophysical JournalPeer-reviewed·Apr 24, 2024
- HP1 dimerization drives the condensation and segregation of H3K9me-marked chromatin
Karthik Eswara, Jennifer I. Semple, … Wolfgang Fischle·bioRxiv·Nov 13, 2025
- The role of electrostatic interactions in the phase separation of HP1α and its protein binding partners
Cheenou Her, Rushabh Bhakta, … Galia T. Debelouchina·bioRxiv·Jul 8, 2026
- HP1 proteins compact DNA into mechanically and positionally stable phase separated domains
M. M. Keenen, D. Brown, … S. Redding·bioRxiv·Oct 30, 2020
- Condensate-driven chromatin organization via elastocapillary interactions
Hongbo Zhao, Amy R. Strom, … Clifford P. Brangwynne·bioRxiv·Jun 12, 2025