ArticleMolecular and cellular biology2000
Role of histone N-terminal tails and their acetylation in nucleosome dynamics.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 119 citations in OpenAlex.
- Chromatin Accessibility in Cancer: Biological Functions, Mechanisms, Therapeutic Potential, and Future Directions.MedComm · 2026Review
- Precision epigenetic therapies in oncology.Cancer metastasis reviews · 2025Review
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- Transcriptionally active chromatin loops contain both 'active' and 'inactive' histone modifications that exhibit exclusivity at the level of nucleosome clusters.Epigenetics & chromatin · 2024Article
- Review
- Studies of the Mechanism of Nucleosome Dynamics: A Review on Multifactorial Regulation from Computational and Experimental Cases.Polymers · 2023Review
- Shaking up the silence: consequences of HMGN1 antagonizing PRC2 in the Down syndrome brain.Epigenetics & chromatin · 2022Review
- Mechanical determinants of chromatin topology and gene expression.Nucleus (Austin, Tex.) · 2022Review
- Histone H3 proline 16 hydroxylation regulates mammalian gene expression.Nature genetics · 2022Article
- Review
- Epi-Drugs in Heart Failure.Frontiers in cardiovascular medicine · 2022Review
- EZH2 inhibition: a promising strategy to prevent cancer immune editing.Epigenomics · 2020Review
- Homeostasis of histone acetylation is critical for auxin signaling and root morphogenesis.Plant molecular biology · 2020Review
- p53 at the Crossroads between Different Types of HDAC Inhibitor-Mediated Cancer Cell Death.International journal of molecular sciences · 2019Review
- Epigenetic Targeting of Autophagy via HDAC Inhibition in Tumor Cells: Role of p53.International journal of molecular sciences · 2018Review
- Bivalent Epigenetic Control of Oncofetal Gene Expression in Cancer.Molecular and cellular biology · 2017Review
- Article
- Acetylation Mimics Within a Single Nucleosome Alter Local DNA Accessibility In Compacted Nucleosome Arrays.Scientific reports · 2016Article
- Distinct Roles of Histone H3 and H2A Tails in Nucleosome Stability.Scientific reports · 2016Article
- Poly(ADP-ribose) polymerase-1 silences retroviruses independently of viral DNA integration or heterochromatin formation.The Journal of general virology · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Histone N-terminal tails are central to the processes that modulate nucleosome structure and function. We have studied the contribution of core histone tails to the structure of a single nucleosome and to a histone (H3-H4)(2) tetrameric particle assembled on a topologically constrained DNA minicircle. The effect of histone tail cleavage and histone tail acetylation on the structure of the nucleoprotein particle was investigated by analyzing the DNA topoisomer equilibrium after relaxation of DNA torsional stress by topoisomerase I. Removal of the H3 and H4 N-terminal tails, as well as their acetylation, provoked a dramatic change in the linking-number difference of the (H3-H4)(2) tetrameric particle, with a release of up to 70% of the negative supercoiling previously constrained by this structure. The (H3-H4)(2) tetramers containing tailless or hyperacetylated histones showed a striking preference for relaxed DNA over negatively supercoiled DNA. This argues in favor of a change in tetramer structure that constrains less DNA and adopts a relaxed flat conformation instead of its left-handed conformation within the nucleosome. In contrast neither removal or hyperacetylation of H3 and H4 tails nor removal or hyperacetylation of H2A and H2B N-terminal tails affected the nucleosome structure. This indicates that the globular domain of H2A and H2B is sufficient to stabilize the tailless or the hyperacetylated (H3-H4)(2) tetramer in a left-handed superhelix conformation. These results suggest that the effect of histone tail acetylation that facilitates transcription may be mediated via transient formation of an (H3-H4)(2) tetrameric particle that could adopt an open structure only when H3 and/or H4 tails are hyperacetylated.
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