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Related Concept Videos

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
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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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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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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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Effects of Histone H2B Ubiquitylations and H3K79me<sub>3</sub> on Transcription Elongation.

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Related Experiment Video

Updated: Jan 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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Ubiquitylation: How Nucleosomes Use Histones to Evict Histones.

Wladyslaw A Krajewski1

  • 1N.K. Koltsov Institute of Developmental Biology of Russian Academy of Sciences, Vavilova str. 26, Moscow, 119334, Russia.

Trends in Cell Biology
|July 7, 2019
PubMed
Summary

Bulky histone modifications, like ubiquitylation, can directly destabilize nucleosome structure. This offers a new way bulky modifications regulate chromatin, separate from recruiting other proteins.

Keywords:
chromatinhexasomehistone codehistone modificationsnucleosomeubiquitylation

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Dynamics

Background:

  • Histone modifications are key regulators of gene expression.
  • Their established roles involve recruiting effector proteins and altering DNA accessibility via charge shielding.
  • The direct physical impact of modifications on chromatin structure is less understood.

Purpose of the Study:

  • To investigate the direct structural impact of bulky histone modifications on nucleosome stability.
  • To explore a novel mechanism of chromatin regulation independent of effector recruitment.

Main Methods:

  • Utilizing structural biology techniques to analyze nucleosome remodeling.
  • Investigating the effects of specific bulky histone modifications, such as ubiquitylation.

Main Results:

  • Steric hindrance from bulky histone modifications, exemplified by ubiquitylation, was shown to destabilize canonical nucleosome structure.
  • This destabilization directly impacts chromatin organization.

Conclusions:

  • Bulky histone modifications can directly remodel nucleosome structure through steric effects.
  • This represents a novel mechanism of chromatin regulation distinct from established models.