ArticleScientific reports2015
Intra- and inter-nucleosomal interactions of the histone H4 tail revealed with a human nucleosome core particle with genetically-incorporated H4 tetra-acetylation.
Article in Scientific reports, 2015. 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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50 citing papers in PubMed, 84 citations in OpenAlex.
- Linker histone H1 represses H3 tail acetylation induced by H4 tail acetylation and alters its dynamics.Communications biology · 2026Article
- Time-Resolved Single-Molecule FRET Reveals Length-Dependent Nucleosome Decompaction by Poly(ADP-ribose).bioRxiv : the preprint server for biology · 2026Article
- H4K16 acylations destabilize chromatin architecture and facilitate transcriptional response during metabolic perturbations.Molecular cell · 2026Article
- Dynamic networks of intrinsically disordered regions in nuclear proteins.Biophysics and physicobiology · 2026Article
- Gene-scale in vitro reconstitution reveals histone acetylation directly controls chromatin architecture.Science advances · 2025Article
- Structural insights into γH2Ax containing nucleosomes.Nucleic acids research · 2025Article
- Timed chromatin invasion during mitosis governs prototype foamy virus integration site selection and infectivity.Nucleic acids research · 2025Article
- An Oryza-specific histone H4 variant predisposes H4 lysine 5 acetylation to modulate salt stress responses.Nature plants · 2025Article
- Molecular Dynamics Simulations of Nucleosomes Containing Histone Variant H2A.J.International journal of molecular sciences · 2024Article
- The Free Energy of Nucleosomal DNA Based on the Landau Model and Topology.Biomolecules · 2023Article
- Structural basis of telomeric nucleosome recognition by shelterin factor TRF1.Science advances · 2023Article
- Epigenetic mechanisms to propagate histone acetylation by p300/CBP.Nature communications · 2023Article
- Histone H3 lysine 27 crotonylation mediates gene transcriptional repression in chromatin.Molecular cell · 2023Article
- The role of auxiliary domains in modulating CHD4 activity suggests mechanistic commonality between enzyme families.Nature communications · 2022Article
- Review
- Characteristic H3 N-tail dynamics in the nucleosome core particle, nucleosome, and chromatosome.iScience · 2022Article
- Structural basis of chromatin regulation by histone variant H2A.Z.Nucleic acids research · 2021Article
- The structure of a virus-encoded nucleosome.Nature structural & molecular biology · 2021Article
- Histone tails as signaling antennas of chromatin.Current opinion in structural biology · 2021Review
- Histone H4 Tails in Nucleosomes: a Fuzzy Interaction with DNA.Angewandte Chemie (International ed. in English) · 2021Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications (PTMs) of histones, such as lysine acetylation of the N-terminal tails, play crucial roles in controlling gene expression. Due to the difficulty in reconstituting site-specifically acetylated nucleosomes with crystallization quality, structural analyses of histone acetylation are currently performed using synthesized tail peptides. Through engineering of the genetic code, translation termination, and cell-free protein synthesis, we reconstituted human H4-mono- to tetra-acetylated nucleosome core particles (NCPs), and solved the crystal structures of the H4-K5/K8/K12/K16-tetra-acetylated NCP and unmodified NCP at 2.4 Å and 2.2 Å resolutions, respectively. The structure of the H4-tetra-acetylated NCP resembled that of the unmodified NCP, and the DNA wrapped the histone octamer as precisely as in the unmodified NCP. However, the B-factors were significantly increased for the peripheral DNAs near the N-terminal tail of the intra- or inter-nucleosomal H4. In contrast, the B-factors were negligibly affected by the H4 tetra-acetylation in histone core residues, including those composing the acidic patch, and at H4-R23, which interacts with the acidic patch of the neighboring NCP. The present study revealed that the H4 tetra-acetylation impairs NCP self-association by changing the interactions of the H4 tail with DNA, and is the first demonstration of crystallization quality NCPs reconstituted with genuine PTMs.
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