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Related Concept Videos

Histone Modification02:32

Histone Modification

14.6K
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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Histone Variants at the Centromere02:30

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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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Spreading of Chromatin Modifications02:25

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
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Position-effect Variegation02:32

Position-effect Variegation

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In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
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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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Related Experiment Video

Updated: May 1, 2026

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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Histone variants: dynamic punctuation in transcription.

Christopher M Weber1, Steven Henikoff

  • 1Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA;

Genes & Development
|April 4, 2014
PubMed
Summary

Histone variants dynamically regulate gene expression by altering nucleosome structure and DNA accessibility. These changes create unique chromatin states essential for transcriptional control in eukaryotes.

Keywords:
gene regulationhistone chaperonesnucleosome dynamicsnucleosome remodeling

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Area of Science:

  • Molecular Biology
  • Genetics
  • Epigenetics

Background:

  • Eukaryotic gene regulation requires balancing genome packaging with accessibility for proteins.
  • Nucleosomes, formed by histones, control access to regulatory DNA sequences.
  • Canonical histones package DNA, but variants can modify nucleosome properties.

Purpose of the Study:

  • To explore the role of histone variants and their partners in transcriptional regulation.
  • To understand how unique chromatin states are established by histone variants.

Main Methods:

  • Review of literature on histone variants and chromatin structure.
  • Analysis of mechanisms by which histone variants influence DNA accessibility.
  • Examination of protein interactions with histone variants.

Main Results:

  • Histone variants alter nucleosome structure, stability, and dynamics.
  • These alterations directly impact DNA accessibility for regulatory factors.
  • Specific histone variants and interacting proteins contribute to distinct chromatin states.

Conclusions:

  • Histone variants are key regulators of eukaryotic gene expression.
  • They modulate chromatin accessibility, influencing transcriptional outcomes.
  • The interplay between histone variants and partners defines functional chromatin states.