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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...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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...

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Related Experiment Video

Updated: May 22, 2026

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

Histone H3 phosphorylation - a versatile chromatin modification for different occasions.

Anna Sawicka1, Christian Seiser

  • 1Department of Medical Biochemistry, Max F. Perutz Laboratories, Vienna Biocenter, Medical University of Vienna, Dr. Bohr-Gasse 9/2, A-1030 Vienna, Austria.

Biochimie
|May 9, 2012
PubMed
Summary

Histone H3 phosphorylation dynamically regulates gene activity and chromatin structure. This modification, alongside other histone marks, influences gene activation and silencing, impacting epigenetic memory.

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

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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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Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

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Last Updated: May 22, 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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Published on: May 17, 2016

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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Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Genomics

Background:

  • Post-translational modifications (PTMs) of histones are crucial for regulating chromatin accessibility and gene transcription in eukaryotes.
  • Histone H3 phosphorylation plays a dual role, correlating with both active gene transcription and mitotic chromatin condensation.
  • Combinatorial patterns of histone H3 phosphorylation with acetylation and methylation are recognized by specific protein readers.

Purpose of the Study:

  • To review the significance of various histone H3 phosphorylation marks in chromatin condensation during mitosis.
  • To examine the triggers and regulatory factors of histone H3 phosphorylation during interphase and its biological readout.
  • To discuss models for histone H3 phosphorylation's role in activating poised genes and transiently derepressing silenced genes.

Main Methods:

  • Literature review focusing on histone H3 phosphorylation.
  • Analysis of signaling pathways that initiate histone H3 phosphorylation.
  • Examination of protein factors controlling reversible histone H3 phosphorylation.
  • Discussion of models for histone H3 phosphorylation's role in gene regulation.

Main Results:

  • Histone H3 phosphorylation is a dynamic PTM involved in both gene activation and chromatin condensation.
  • Specific phosphorylation marks on histone H3, in conjunction with other PTMs, create unique epigenetic signatures.
  • Histone H3 phosphorylation is triggered by specific signals and reversibly controlled by regulatory factors during the cell cycle.

Conclusions:

  • Histone H3 phosphorylation is a key regulator of chromatin structure and gene expression.
  • The interplay between histone H3 phosphorylation and lysine methylation may transiently override gene silencing without erasing epigenetic memory.
  • Understanding these modifications provides insights into gene activation and epigenetic regulation.