ArticleJournal of the American Chemical Society2013
Histone H3 and H4 N-terminal tails in nucleosome arrays at cellular concentrations probed by magic angle spinning NMR spectroscopy.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed.
- DNA Sequence and Histone Variant H2A.Z Jointly Govern Nucleosome Unwrapping Pathways.bioRxiv : the preprint server for biology · 2026Article
- H2A.Z facilitates Sox2-nucleosome interaction by promoting DNA and histone H3 tail mobility.Nucleic acids research · 2026Article
- Characterization of intrinsically disordered regions through scalar coupling-based solid-state NMR experiments.Biophysics reports · 2025Article
- Semisynthesis of Isomerized Histone H4 Reveals Robustness and Vulnerability of Chromatin toward Molecular Aging.Journal of the American Chemical Society · 2025Article
- From molecular descriptions to cellular functions of intrinsically disordered protein regions.Biophysics reviews · 2024Review
- Structural and dynamic studies of chromatin by solid-state NMR spectroscopy.Current opinion in structural biology · 2024Review
- Unveiling structural and dynamical features of chromatin using NMR spectroscopy.Magnetic resonance letters · 2024Review
- Structural dynamics in chromatin unraveling by pioneer transcription factors.Biophysical reviews · 2024Review
- Phosphorylation regulates tau's phase separation behavior and interactions with chromatin.Communications biology · 2024Article
- Article
- Using NMR diffusion data to validate MD models of disordered proteins: Test case of N-terminal tail of histone H4.Biophysical journal · 2024Article
- Phosphorylation regulates tau's phase separation behavior and interactions with chromatin.bioRxiv : the preprint server for biology · 2023Article
- Conformational and Interaction Landscape of Histone H4 Tails in Nucleosomes Probed by Paramagnetic NMR Spectroscopy.Journal of the American Chemical Society · 2023Article
- Structural and dynamical investigation of histone H2B in well-hydrated nucleosome core particles by solid-state NMR.Communications biology · 2023Article
- The effects of RNA.DNA-DNA triple helices on nucleosome structures and dynamics.Biophysical journal · 2023Article
- Arginine anchor points govern H3 tail dynamics.Frontiers in molecular biosciences · 2023Article
- Probing Watson-Crick and Hoogsteen base pairing in duplex DNA using dynamic nuclear polarization solid-state NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- DNP-enhanced solid-state NMR spectroscopy of chromatin polymers.Journal of magnetic resonance open · 2022Article
- Untargeted 2D NMR Metabolomics of [Journal of proteome research · 2022Article
- Visualizing Conformational Ensembles of the Nucleosome by NMR.ACS chemical biology · 2022Review
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Authors and funding
7 authors.
Funding
Abstract
Chromatin is a supramolecular assembly of DNA and histone proteins, organized into nucleosome repeat units. The dynamics of chromatin organization regulates DNA accessibility to eukaryotic transcription and DNA repair complexes. Yet, the structural and dynamic properties of chromatin at high concentrations characteristic of the cellular environment (>∼200 mg/mL) are largely unexplored at the molecular level. Here, we apply MAS NMR to directly probe the dynamic histone protein regions in (13)C,(15)N-enriched recombinant nucleosome arrays at cellular chromatin concentrations and conditions designed to emulate distinct states of DNA condensation, with focus on the flexible H3 and H4 N-terminal tails which mediate chromatin compaction. 2D (1)H-(13)C and (1)H-(15)N spectra reveal numerous correlations for H3 and H4 backbone and side-chain atoms, enabling identification of specific residues making up the dynamically disordered N-terminal tail domains. Remarkably, we find that both the H3 and H4 N-terminal tails are overall dynamic even in a highly condensed state. This significant conformational flexibility of the histone tails suggests that they remain available for protein binding in compact chromatin states to enable regulation of heterochromatin. Furthermore, our study provides a foundation for quantitative structural and dynamic investigations of chromatin at physiological concentrations.
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