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Related Concept Videos

The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.7K
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

Histone Modification

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The Nucleosome01:19

The Nucleosome

4.8K
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.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
4.8K
The Nucleosome02:33

The Nucleosome

19.9K
DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to 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.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
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Related Experiment Video

Updated: Apr 7, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

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Histone core phosphorylation regulates DNA accessibility.

Matthew Brehove1, Tao Wang2, Justin North3

  • 1From the Department of Physics.

The Journal of Biological Chemistry
|July 16, 2015
PubMed
Summary

Histone phosphorylation at tyrosine 41 (H3Y41ph) and H3K56 acetylation (H3K56ac) significantly increase DNA accessibility within nucleosomes. Their combined effect enhances DNA access for transcription regulatory complexes.

Keywords:
DNA accessibilityDNA-protein interactionfluorescence resonance energy transfer (FRET)histone modificationhistone post-translational modificationsnucleosomesmall-angle X-ray scattering (SAXS)

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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Structure

Background:

  • Nucleosome unwrapping dynamics control access to DNA for crucial cellular processes like transcription, repair, and replication.
  • Histone H3 modifications, specifically phosphorylation at tyrosine 41 (H3Y41ph) and threonine 45 (H3T45ph), are located at the DNA-histone interface and may influence DNA accessibility.
  • The role of histone phosphorylation in modulating nucleosome unwrapping and DNA accessibility remains largely unexplored.

Purpose of the Study:

  • To investigate the impact of histone H3 phosphorylation, particularly H3Y41ph, on nucleosome unwrapping and DNA accessibility.
  • To explore the effect of H3K56 acetylation (H3K56ac) on nucleosome unwrapping and DNA accessibility.
  • To determine the combined effect of H3Y41ph and H3K56ac on DNA accessibility.

Main Methods:

  • Utilized phosphorylation mimics (H3Y41E, H3T45E) and the chemically correct modification (H3Y41ph) to study histone H3 phosphorylation.
  • Assessed nucleosome unwrapping dynamics and DNA accessibility using biophysical techniques.
  • Investigated the synergistic effects of H3Y41ph and H3K56ac on DNA accessibility.

Main Results:

  • H3Y41ph significantly increases nucleosome unwrapping, enhancing DNA accessibility to protein binding by approximately 3-fold.
  • H3K56ac also promotes DNA unwrapping and increases DNA accessibility.
  • The combination of H3Y41ph and H3K56ac dramatically increases DNA accessibility by over an order of magnitude.

Conclusions:

  • Phosphorylation of histone H3 within the nucleosome's DNA entry-exit region enhances access for DNA-binding complexes.
  • The synergistic action of H3Y41ph and H3K56ac has a profound impact on DNA accessibility, potentially playing a critical role in regulating transcription.
  • These findings highlight a novel mechanism by which epigenetic modifications influence DNA accessibility and gene regulation.