ArticlePLoS genetics2009
Interaction of HP1 and Brg1/Brm with the globular domain of histone H3 is required for HP1-mediated repression.
Article in PLoS genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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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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Who cites it
50 citing papers in PubMed, 88 citations in OpenAlex.
- In vitro reconstitution of heterochromatin compartments reveals the spontaneous formation of tunable liquid-liquid interfaces.Nucleic acids research · 2026Article
- SMARCA4 regulates SMARCAD1 expression for toleration of replication stress in non-small cell lung cancer.Fujita medical journal · 2026Article
- Review
- HP1a promotes chromatin liquidity and drives spontaneous heterochromatin compartmentalization.bioRxiv : the preprint server for biology · 2025Article
- Heterochromatic gene silencing controls CD4Nature communications · 2025Article
- Heterochromatin protein 1 alpha (HP1α) undergoes a monomer to dimer transition that opens and compacts live cell genome architecture.Nucleic acids research · 2024Article
- Heterochromatic 3D genome organization is directed by HP1a- and H3K9-dependent and independent mechanisms.Molecular cell · 2024Article
- Phosphorylated HP1α-Nucleosome Interactions in Phase Separated Environments.Journal of the American Chemical Society · 2023Article
- New twists of a TAIL: novel insights into the histone binding properties of a highly conserved PHD finger cluster within the MLR family of H3K4 mono-methyltransferases.Nucleic acids research · 2023Article
- Catalytic and non-catalytic mechanisms of histone H4 lysine 20 methyltransferase SUV420H1.bioRxiv : the preprint server for biology · 2023Article
- Molecular interactions underlying the phase separation of HP1α: role of phosphorylation, ligand and nucleic acid binding.Nucleic acids research · 2022Article
- HP1β carries an acidic linker domain and requires H3K9me3 for phase separation.Nucleus (Austin, Tex.) · 2021Article
- Phosphorylation of the HP1β hinge region sequesters KAP1 in heterochromatin and promotes the exit from naïve pluripotency.Nucleic acids research · 2021Article
- Interferons: Tug of War Between Bacteria and Their Host.Frontiers in cellular and infection microbiology · 2021Review
- Biology and Physics of Heterochromatin-Cells · 2020Review
- Heterochromatin protein 1 (HP1): interactions with itself and chromatin components.Biophysical reviews · 2020Review
- On the relations of phase separation and Hi-C maps to epigenetics.Royal Society open science · 2020Article
- BRM: the core ATPase subunit of SWI/SNF chromatin-remodelling complex-a tumour suppressor or tumour-promoting factor?Epigenetics & chromatin · 2019Review
- Article
- Biophysical Properties of HP1-Mediated Heterochromatin.Cold Spring Harbor symposia on quantitative biology · 2019Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
The heterochromatin-enriched HP1 proteins play a critical role in regulation of transcription. These proteins contain two related domains known as the chromo- and the chromoshadow-domain. The chromo-domain binds histone H3 tails methylated on lysine 9. However, in vivo and in vitro experiments have shown that the affinity of HP1 proteins to native methylated chromatin is relatively poor and that the opening of chromatin occurring during DNA replication facilitates their binding to nucleosomes. These observations prompted us to investigate whether HP1 proteins have additional histone binding activities, envisioning also affinity for regions potentially occluded by the nucleosome structure. We find that the chromoshadow-domain interacts with histone H3 in a region located partially inside the nucleosomal barrel at the entry/exit point of the nucleosome. Interestingly, this region is also contacted by the catalytic subunits of the human SWI/SNF complex. In vitro, efficient SWI/SNF remodeling requires this contact and is inhibited in the presence of HP1 proteins. The antagonism between SWI/SNF and HP1 proteins is also observed in vivo on a series of interferon-regulated genes. Finally, we show that SWI/SNF activity favors loading of HP1 proteins to chromatin both in vivo and in vitro. Altogether, our data suggest that HP1 chromoshadow-domains can benefit from the opening of nucleosomal structures to bind chromatin and that HP1 proteins use this property to detect and arrest unwanted chromatin remodeling.
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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.