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Related Concept Videos

The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
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The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
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Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Histone Modification02:32

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Nucleosome Remodeling02:54

Nucleosome Remodeling

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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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The Nucleosome01:19

The Nucleosome

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Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
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Related Experiment Video

Updated: Apr 22, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

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Histone core modifications regulating nucleosome structure and dynamics.

Peter Tessarz1, Tony Kouzarides2

  • 1Gurdon Institute and Department of Pathology, Tennis Court Road, Cambridge, CB2 1QN, UK; and the Max Planck Research Group 'Chromatin and Ageing', Max Planck Institute for Biology of Ageing, Joseph-Stelzmann-Strasse 9b, 50931 Cologne, Germany.

Nature Reviews. Molecular Cell Biology
|October 16, 2014
PubMed
Summary
This summary is machine-generated.

Histone post-translational modifications regulate DNA processes by recruiting proteins and directly impacting chromatin structure. These modifications influence DNA-protein interactions and histone chaperone binding, affecting nucleosomal architecture.

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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

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Area of Science:

  • Epigenetics and Molecular Biology
  • Chromatin Biology
  • Genetics

Background:

  • Post-translational modifications (PTMs) of histones are crucial regulators of DNA-templated processes.
  • These modifications serve as binding platforms for effector proteins like transcriptional regulators and chromatin remodelers.
  • Emerging evidence indicates PTMs directly influence nucleosomal architecture.

Purpose of the Study:

  • To explore the direct impact of histone PTMs on nucleosomal structure.
  • To elucidate how histone modifications affect chromatin organization and function.
  • To understand the molecular mechanisms underlying PTM-mediated chromatin modulation.

Main Methods:

  • Review of recent literature on histone modifications and chromatin structure.
  • Analysis of experimental data demonstrating PTM effects on nucleosomes.
  • Computational modeling of histone-DNA and histone-histone interactions.

Main Results:

  • Histone PTMs, including acetylation, methylation, phosphorylation, and citrullination, directly alter nucleosomal architecture.
  • These modifications impact histone-histone and histone-DNA interactions.
  • PTMs influence the binding of histones to molecular chaperones.

Conclusions:

  • Histone PTMs play a dual role: recruiting effector proteins and directly modulating chromatin structure.
  • Understanding these direct structural effects is key to comprehending gene regulation and DNA processing.
  • Further research into PTM-mediated structural changes will illuminate epigenetic mechanisms.