ArticleNucleic acids research2020
Acetylation-modulated communication between the H3 N-terminal tail domain and the intrinsically disordered H1 C-terminal domain.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Linker Histones: The Multiple Binding Modes of the Enigmatic 5th Histone.Biomolecules · 2026Review
- Conformations of Linker Histone H1 Bound to Nucleosome Arrays.Journal of molecular biology · 2026Article
- Roles of histone chaperone Nap1 and histone acetylation in regulating phase-separation of nucleosome arrays.Nature communications · 2025Article
- An integrated analysis of second- and third-generation transcriptome sequencing technologies reveals theAnimal reproduction · 2025Article
- Unveiling the mysteries of extrachromosomal circular DNA: from generation to clinical relevance in human cancers and health.Molecular cancer · 2024Review
- Circular Engineered Sortase for Interrogating Histone H3 in Chromatin.Journal of the American Chemical Society · 2024Article
- A circular engineered sortase for interrogating histone H3 in chromatin.bioRxiv : the preprint server for biology · 2024Article
- Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II.Nucleic acids research · 2023Article
- Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes.Journal of molecular biology · 2023Article
- Article
- Review
- Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021Review
- Transcriptionally Active Chromatin-Lessons Learned from the Chicken Erythrocyte Chromatin Fractionation.Cells · 2021Review
- Intestinal differentiation involves cleavage of histone H3 N-terminal tails by multiple proteases.Nucleic acids research · 2021Article
- Proximal-end bias from in-vitro reconstituted nucleosomes and the result on downstream data analysis.PloS one · 2021Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Linker histones (H1s) are key structural components of the chromatin of higher eukaryotes. However, the mechanisms by which the intrinsically disordered linker histone carboxy-terminal domain (H1 CTD) influences chromatin structure and gene regulation remain unclear. We previously demonstrated that the CTD of H1.0 undergoes a significant condensation (reduction of end-to-end distance) upon binding to nucleosomes, consistent with a transition to an ordered structure or ensemble of structures. Here, we show that deletion of the H3 N-terminal tail or the installation of acetylation mimics or bona fide acetylation within H3 N-terminal tail alters the condensation of the nucleosome-bound H1 CTD. Additionally, we present evidence that the H3 N-tail influences H1 CTD condensation through direct protein-protein interaction, rather than alterations in linker DNA trajectory. These results support an emerging hypothesis wherein the H1 CTD serves as a nexus for signaling in the nucleosome.
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