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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
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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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The Nucleosome02:33

The Nucleosome

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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.
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The Nucleosome02:33

The Nucleosome

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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.
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Related Experiment Video

Updated: May 6, 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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Structural insights into the histone H1-nucleosome complex.

Bing-Rui Zhou1, Hanqiao Feng, Hidenori Kato

  • 1Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.

Proceedings of the National Academy of Sciences of the United States of America
|November 13, 2013
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Summary

Linker histone H1

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Area of Science:

  • Molecular Biology
  • Chromatin Structure
  • Biophysics

Background:

  • Linker histones (H1) are crucial for higher-order chromatin organization and cellular functions.
  • The precise structural interactions between H1 and nucleosomes remain largely unknown.
  • Understanding H1-nucleosome interactions is key to deciphering chromatin dynamics.

Purpose of the Study:

  • To elucidate the structural basis of the interaction between Drosophila H1 and the nucleosome.
  • To develop a residue-specific structural model of the H1-nucleosome complex.

Main Methods:

  • Solution nuclear magnetic resonance (NMR) spectroscopy.
  • Biophysical techniques.
  • Structural modeling.

Main Results:

  • The globular domain of H1 asymmetrically bridges the nucleosome core and linker DNA.
  • The H1 α3 helix interacts with nucleosomal DNA near the dyad axis.
  • Specific regions of H1 C-terminal tail and H2A C-terminal tail contribute to complex formation.

Conclusions:

  • A novel, residue-specific structural model for the Drosophila H1-nucleosome complex was determined.
  • This model differs significantly from previously proposed structures.
  • The findings provide new insights into chromatin higher-order structure and dynamics.