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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...
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...
Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying DNA...

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Related Experiment Video

Updated: May 16, 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

One, two, three: how histone methylation is read.

Wolfgang Fischle1

  • 1Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. wfischl@gwdg.de

Epigenomics
|December 19, 2012
PubMed
Summary
This summary is machine-generated.

Histone methylation, a key epigenetic mechanism, involves specific proteins that read and translate these marks, influencing genome function. Understanding these interactions reveals complex regulatory networks controlling gene expression.

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Analysis of Histone Antibody Specificity with Peptide Microarrays
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Analysis of Histone Antibody Specificity with Peptide Microarrays

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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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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

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Related Experiment Videos

Last Updated: May 16, 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

Published on: January 26, 2018

Analysis of Histone Antibody Specificity with Peptide Microarrays
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Analysis of Histone Antibody Specificity with Peptide Microarrays

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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Area of Science:

  • Epigenetics and Molecular Biology

Background:

  • Histone methylation is a complex epigenetic regulatory system.
  • Methylation marks on histone lysine and arginine residues have significant signaling potential and stability.
  • These marks are integral components of epigenetic regulatory networks.

Purpose of the Study:

  • To elucidate the biological principles of how histone methylation marks are read and translated.
  • To identify and characterize histone methylation binding proteins and their interaction mechanisms.
  • To understand the regulatory patterns of these binding proteins.

Main Methods:

  • Identification and characterization of histone methylation binding proteins.
  • Analysis of specialized protein modules involved in methylation site- and state-specific chromatin recruitment.
  • Investigation of molecular interaction mechanisms between histone marks and binding proteins.

Main Results:

  • Few histone methyl marks directly impact chromatin structure.
  • A large number of histone methylation binding proteins have been identified.
  • These proteins possess specialized modules for specific recruitment to chromatin.
  • Molecular mechanisms of interaction and regulatory patterns are becoming evident.

Conclusions:

  • Histone methylation is a critical epigenetic mechanism involving specific binding proteins.
  • These proteins translate methylation signals through specialized modules for chromatin regulation.
  • Further research into these interactions will illuminate complex epigenetic regulatory networks.