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Related Concept Videos

Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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 is an enzyme that can...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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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Related Experiment Video

Updated: May 9, 2026

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
07:20

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

Histone variants in development and diseases.

Ping Chen1, Jicheng Zhao, Guohong Li

  • 1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Journal of Genetics and Genomics = Yi Chuan Xue Bao
|July 24, 2013
PubMed
Summary
This summary is machine-generated.

Histone variants like H2A.Z, macroH2A, and H3.3 regulate chromatin structure and gene expression. Understanding their epigenetic roles is crucial for development, aging, and disease research.

Keywords:
DevelopmentDiseasesEpigenetic regulationHigher-order chromatin structureHistone variant

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Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

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Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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Published on: May 5, 2022

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
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Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Genetics

Background:

  • Eukaryotic DNA is packaged into chromatin by histones.
  • Histone variants possess distinct regulatory mechanisms, impacting chromatin plasticity and function.
  • The precise mechanisms of histone variant incorporation and their roles in development and disease are not fully understood.

Purpose of the Study:

  • To review recent advances in understanding the epigenetic regulation of key histone variants.
  • To explore the functional implications of histone variants in development and diseases.
  • To highlight the roles of H2A.Z, macroH2A, and H3.3 in chromatin regulation.

Main Methods:

  • Literature review focusing on epigenetic regulation studies.
  • Analysis of research on histone variant expression, deposition, and function.
  • Synthesis of findings related to H2A.Z, macroH2A, and H3.3.

Main Results:

  • Histone variants contribute to diverse chromatin structures and functional domains.
  • Specific variants like H2A.Z, macroH2A, and H3.3 are implicated in critical biological processes.
  • Epigenetic regulation of these variants influences gene expression, development, and disease states.

Conclusions:

  • Histone variants are key players in chromatin dynamics and epigenetic control.
  • Further investigation into histone variant mechanisms is essential for understanding development and disease.
  • H2A.Z, macroH2A, and H3.3 represent critical areas for future epigenetic research.