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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...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
Epigenetic Regulation01:37

Epigenetic Regulation

Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...
Epigenetic Regulation01:46

Epigenetic Regulation

Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.

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Related Experiment Video

Updated: Jun 4, 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

Selective targeting of histone methylation.

Abul B M M K Islam1, William F Richter, Nuria Lopez-Bigas

  • 1Research Unit on Biomedical Informatics, Department of Experimental Health and Sciences, PRBB, Universitat Pompeu Fabra, Barcelona, Spain.

Cell Cycle (Georgetown, Tex.)
|January 29, 2011
PubMed
Summary

Histone-modifying enzymes regulate gene expression. This study reveals how enzymes placing histone H3 lysine 4 (H3K4) and histone H3 lysine 27 (H3K27) marks are recruited, showing coordinated, opposed, or alternating binding patterns.

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Last Updated: Jun 4, 2026

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

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Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae
11:06

Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae

Published on: December 29, 2017

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • Histones are crucial for gene expression regulation through post-translational modifications.
  • Histone-modifying enzymes are key players, but their in vivo recruitment mechanisms are not fully understood.
  • Genome-wide methods offer insights into enzyme recruitment and differential gene expression patterns.

Purpose of the Study:

  • To investigate the recruitment mechanisms of enzymes involved in histone H3 lysine 4 (H3K4) methylation and histone H3 lysine 27 (H3K27) methylation.
  • To analyze the distribution and interplay of binding sites for these contrasting histone mark enzymes.
  • To understand how enzyme recruitment contributes to establishing differential gene expression.

Main Methods:

  • Focus on genome-wide recruitment patterns of histone-modifying enzymes.
  • Analysis of binding site distribution for H3K4 and H3K27 modifying enzymes.
  • Investigation of enzyme interplay, exemplified by KDM5A and KDM5B.

Main Results:

  • Recruitment of different histone-modifying proteins can be coordinated, opposed, or alternating.
  • Genomic sites of H3K4 demethylase KDM5A become accessible to KDM5B when KDM5A levels are reduced.
  • Evidence suggests sequential and temporal targeting of H3K4/H3K27 modifying enzyme complexes.

Conclusions:

  • Enzyme recruitment for H3K4 and H3K27 marks exhibits complex coordination patterns.
  • KDM5A levels influence KDM5B accessibility, highlighting enzyme interdependence.
  • While sequential targeting is suggested, unknown interactions likely contribute to specificity in histone modification enzyme recruitment.