ArticleNucleic acids research2024
Heterochromatin protein 1 alpha (HP1α) undergoes a monomer to dimer transition that opens and compacts live cell genome architecture.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Mapping Protein Diffusion from the Plasma Membrane to the Nucleus: Insights from Fluorescence Correlation Spectroscopy.Biomolecules · 2026Review
- The novel HP1a interactor Clump/CG30403 safeguards transposon silencing and reproductive resilience in thebioRxiv : the preprint server for biology · 2026Article
- The role of electrostatic interactions in the phase separation of HP1α and its protein binding partners.bioRxiv : the preprint server for biology · 2026Article
- Replicative senescence induction in single cells is not predicted by telomere length, dysfunction, or oxidation.iScience · 2026Article
- Bound or unbound: mapping and monitoring receptor oligomerization by time-resolved fluorescence live-cell imaging.Frontiers in molecular biosciences · 2026Article
- MORC2 is a phosphorylation-dependent DNA compaction machine.Nature communications · 2025Article
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Authors and funding
14 authors.
Funding
Abstract
Our understanding of heterochromatin nanostructure and its capacity to mediate gene silencing in a living cell has been prevented by the diffraction limit of optical microscopy. Thus, here to overcome this technical hurdle, and directly measure the nucleosome arrangement that underpins this dense chromatin state, we coupled fluorescence lifetime imaging microscopy (FLIM) of Förster resonance energy transfer (FRET) between histones core to the nucleosome, with molecular editing of heterochromatin protein 1 alpha (HP1α). Intriguingly, this super-resolved readout of nanoscale chromatin structure, alongside fluorescence fluctuation spectroscopy (FFS) and FLIM-FRET analysis of HP1α protein-protein interaction, revealed nucleosome arrangement to be differentially regulated by HP1α oligomeric state. Specifically, we found HP1α monomers to impart a previously undescribed global nucleosome spacing throughout genome architecture that is mediated by trimethylation on lysine 9 of histone H3 (H3K9me3) and locally reduced upon HP1α dimerisation. Collectively, these results demonstrate HP1α to impart a dual action on chromatin that increases the dynamic range of nucleosome proximity. We anticipate that this finding will have important implications for our understanding of how live cell heterochromatin structure regulates genome function.
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