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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 deacetylase,...

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 deacetylase,...

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 is an enzyme that can...

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Related Experiment Video

Updated: May 16, 2026

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

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

Systematic analysis of histone modification readout.

Miroslav Nikolov¹, Wolfgang Fischle

¹Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

Molecular Biosystems

|December 6, 2012

Summary

This summary is machine-generated.

Cells organize DNA using chromatin, a complex of DNA and histone proteins. Histone modifications, crucial for regulating gene expression, recruit specific proteins to direct chromatin states, influencing genetic processes.

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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 16, 2026

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

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 Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

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Published on: January 12, 2024

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

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
Genetics
Epigenetics

Background:

Eukaryotic cells organize their genomes within the nucleus using chromatin, a complex of DNA and histone proteins.
Chromatin serves as a regulatory platform for essential genetic processes.
Posttranslational modifications of histone proteins are key regulators of chromatin states and gene expression.

Purpose of the Study:

To review experimental approaches for determining histone modification readout.
To discuss the complexities of the histone modification regulatory system.
To highlight the role of histone modifications in directing chromatin states.

Main Methods:

Summarizing established experimental approaches for histone modification readout.
Characterizing individual factors that interact with histone marks.
Utilizing global approaches to define the histone modification interactome.

Main Results:

Histone modifications primarily function by recruiting specific binding proteins.
A large number of factors interacting with diverse histone marks have been identified.
Global approaches are being developed to map histone modification interactions.

Conclusions:

Histone modification readout is complex and involves protein recruitment.
Understanding these interactions is crucial for deciphering gene regulation.
Further research is needed to fully elucidate the complexities of this regulatory system.