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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,...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

Updated: May 28, 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

Quantitative proteomic approaches to studying histone modifications.

Barry M Zee¹, Nicolas L Young, Benjamin A Garcia

¹415 Schultz Laboratory, Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.

Current Chemical Genomics

|October 4, 2011

Summary

Histone post-translational modifications (PTMs) regulate gene expression. Mass spectrometry (MS) offers a powerful, unbiased method for high-throughput identification and quantification of these crucial epigenetic marks.

Keywords:

Histone mass spectrometry modification epigenetic.proteomic

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Last Updated: May 28, 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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The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin

The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin

Published on: April 11, 2014

Area of Science:

Epigenetics and Molecular Biology
Proteomics

Background:

Histone post-translational modifications (PTMs) are critical regulators of gene expression and eukaryotic genomic profiles.
Classical methods for studying histone PTMs face technical challenges due to their chemical diversity and complex patterns.

Purpose of the Study:

To review the latest advancements in mass spectrometry (MS) for analyzing histone PTMs.
To highlight MS as a leading platform for unbiased and high-throughput identification and quantification of histone PTMs.
To encourage the integration of proteomic, genomic, and epigenetic research.

Main Methods:

Review of recent literature on mass spectrometry techniques applied to histone PTM analysis.
Discussion of the advantages of MS over traditional methods like immunofluorescence and Western blotting.
Focus on high-throughput identification and quantification strategies.

Main Results:

Mass spectrometry is emerging as the most rigorous and unbiased platform for histone PTM analysis.
MS enables high-throughput identification and quantification, overcoming limitations of classical methods.
Recent developments have significantly advanced the capabilities of MS in this field.

Conclusions:

Mass spectrometry is revolutionizing the study of histone PTMs.
The adoption of MS facilitates deeper understanding of epigenetic regulation.
Integration of MS-based proteomics with genomics and epigenetics is key for future discoveries.