ArticleProceedings of the National Academy of Sciences of the United States of America2023
Correlating histone acetylation with nucleosome core particle dynamics and function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 37 citations in OpenAlex.
- Structural basis of PARP2 recognition of nucleosomal DNA breaks and inhibitor trapping.Nucleic acids research · 2026Article
- Site-specific programming characterizes dynamic post-translational acetylation of histone H2B lysine 108 in mouse embryonic stem cells.Nature communications · 2026Article
- Molecular basis of nick ligation in the nucleosome by DNA Ligase IIIα.Nature communications · 2026Article
- Targeting METTL3 Attenuates Thyroid Inflammatory Injury by Restoring Th17/Treg Balance through a YTHDC2-m6A-Dependent KDR/VEGFA Loop.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Article
- Modulating Nucleosomal H3 Tail Dynamics with Lysine and Serine Modifications.bioRxiv : the preprint server for biology · 2026Article
- High-Yield Production of Modified DNA Enables Structural Analysis of PARP2 Recognition of Nucleosomal Single-Strand Breaks.Journal of molecular biology · 2026Article
- IDPForge: Deep Learning of Proteins with Global and Local Regions of Disorder.bioRxiv : the preprint server for biology · 2026Article
- Conformations of Linker Histone H1 Bound to Nucleosome Arrays.Journal of molecular biology · 2026Article
- Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026Review
- Transient histone deacetylase inhibition reveals cell type invariant and specific effects of chromatin decondensation on irradiation response.Frontiers in cell and developmental biology · 2026Article
- Article
- Epigenetic Mechanisms in Autoimmune Thyroid Diseases: Bridging Research and Clinical Applications.International journal of molecular sciences · 2025Review
- Arabidopsis TRB Proteins Form Two Closely Related Complexes to Mediate H3K4me3 Demethylation and Transcriptional Repression.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Roles of histone chaperone Nap1 and histone acetylation in regulating phase-separation of nucleosome arrays.Nature communications · 2025Article
- Residue-Resolved Liquid-State Hyperpolarized NMR of Peptide Condensate Surfaces.Journal of the American Chemical Society · 2025Article
- Circulating Cell-free DNA Fragmentomics Detection and Beyond.Aging and disease · 2025Review
- Heteroaryl-Capped Hydroxamic Acid Derivatives with Varied Linkers: Synthesis and Anticancer Evaluation with Various Apoptosis Analyses in Breast Cancer Cells, Including Docking, Simulation, DFT, and ADMET Studies.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Modulation of histone tail electrostatic potentials in nucleosome core particles by acetylation and PARylation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Unveiling the Conformational Dynamics of the Histone Tails Using Markov State Modeling.Journal of chemical theory and computation · 2025Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Epigenetic modifications of chromatin play a critical role in regulating the fidelity of the genetic code and in controlling the translation of genetic information into the protein components of the cell. One key posttranslational modification is acetylation of histone lysine residues. Molecular dynamics simulations, and to a smaller extent experiment, have established that lysine acetylation increases the dynamics of histone tails. However, a systematic, atomic resolution experimental investigation of how this epigenetic mark, focusing on one histone at a time, influences the structural dynamics of the nucleosome beyond the tails, and how this translates into accessibility of protein factors such as ligases and nucleases, has yet to be performed. Herein, using NMR spectroscopy of nucleosome core particles (NCPs), we evaluate the effects of acetylation of each histone on tail and core dynamics. We show that for histones H2B, H3, and H4, the histone core particle dynamics are little changed, even though the tails have increased amplitude motions. In contrast, significant increases to H2A dynamics are observed upon acetylation of this histone, with the docking domain and L1 loop particularly affected, correlating with increased susceptibility of NCPs to nuclease digestion and more robust ligation of nicked DNA. Dynamic light scattering experiments establish that acetylation decreases inter-NCP interactions in a histone-dependent manner and facilitates the development of a thermodynamic model for NCP stacking. Our data show that different acetylation patterns result in nuanced changes to NCP dynamics, modulating interactions with other protein factors, and ultimately controlling biological output.
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