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Histone Modification

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...

Histone Modification

Histone Modification

Spreading of Chromatin Modifications

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...

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Related Experiment Video

Updated: Mar 30, 2026

Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF

Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF

Published on: January 12, 2024

Affinity reagents for studying histone modifications & guidelines for their quality control.

Goran Kungulovski¹, Rebekka Mauser¹, Albert Jeltsch¹

¹Institute of Biochemistry, Stuttgart University, Pfaffenwaldring 55, 70569 Stuttgart, Germany.

|November 7, 2015

Summary

This review updates quality criteria for histone post-translational modification (PTM) affinity reagents. It evaluates antibodies and recombinant reading domains for reliable chromatin biology research.

Keywords:

ChIP antibodies histone modifications nucleosome quality control reading domains specificity

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Assays for Validating Histone Acetyltransferase Inhibitors

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Area of Science:

Chromatin biology
Molecular biology
Epigenetics

Background:

Histone post-translational modifications (PTMs) regulate crucial chromatin processes.
Accurate detection of histone PTMs is essential for understanding chromatin function.
Current methods rely on affinity reagents like antibodies and recombinant reading domains.

Purpose of the Study:

To evaluate and update quality criteria for assessing the binding specificity of histone PTM affinity reagents.
To discuss the advantages and disadvantages of using antibodies versus recombinant reading domains.
To provide guidance for selecting appropriate reagents in chromatin biology research.

Main Methods:

Review of existing literature on histone PTM detection methods.
Evaluation of quality criteria for affinity reagent specificity.
Comparative analysis of antibodies and recombinant reading domains.

Main Results:

Established approaches for histone PTM characterization depend on affinity reagents.
The performance of these reagents is critical for experimental validity.
Updated quality criteria are proposed for assessing reagent specificity.

Conclusions:

Recombinant reading domains offer advantages like consistent quality and recombinant production.
Antibodies have established roles but can present challenges.
The emerging technology of reading domains holds promise for future chromatin biology research.