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Related Concept Videos

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...
Heterochromatin02:38

Heterochromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...
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: Jun 9, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

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

Published on: January 26, 2018

Decoding the histone H4 lysine 20 methylation mark.

Lata Balakrishnan1, Barry Milavetz

  • 1Department of Biochemistry and Biophysics, University of Rochester, Rochester, NY, USA.

Critical Reviews in Biochemistry and Molecular Biology
|August 26, 2010
PubMed
Summary
This summary is machine-generated.

Histone H4 lysine 20 (H4K20) methylation is crucial for gene regulation and cell division. Ongoing research explores its mechanisms and combinatorial roles in the histone code.

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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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Last Updated: Jun 9, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Published on: January 26, 2018

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

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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

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

Published on: November 30, 2018

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cell Biology

Background:

  • Histone modifications, including H4K20 methylation, are vital for cellular processes.
  • Specific H4K20 methylation states (H4K20me1, H4K20me2, H4K20me3) are linked to transcription, DNA repair, and heterochromatin formation.

Purpose of the Study:

  • To investigate the biological roles and mechanisms of H4K20 methylation.
  • To explore the potential combinatorial interactions of H4K20 methylation with other histone modifications within the histone code.

Main Methods:

  • Literature review and synthesis of current research on H4K20 methylation.
  • Analysis of identified H4K20 methylases and the ongoing search for demethylases.

Main Results:

  • Established links between H4K20me1, H4K20me2, and H4K20me3 and distinct biological functions.
  • Identification of multiple H4K20 methylases, but no known demethylase.

Conclusions:

  • H4K20 methylation plays a significant role in regulating gene expression, DNA repair, and chromatin structure.
  • Further research into H4K20 methylation and the histone code is expected to yield valuable insights into cell division and gene regulation.