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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,...

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Related Experiment Video

Updated: May 21, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

Antibody-free reading of the histone code using a simple chemical sensor array.

Samuel A Minaker¹, Kevin D Daze, Manuel C F Ma

¹Department of Chemistry, University of Victoria, Victoria, British Columbia V8W 3V6, Canada.

Journal of the American Chemical Society

|June 19, 2012

Summary

This study introduces a novel toolkit of dye-displacement sensors for detecting histone modifications. These supramolecular sensors can identify various histone code elements, offering a new method for disease research.

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Area of Science:

Biochemistry
Chemical Biology
Molecular Biology

Background:

The histone code, a network of histone post-translational modifications, regulates gene expression and is implicated in numerous human diseases.
Accurate detection of specific histone modifications is crucial for understanding disease mechanisms.

Purpose of the Study:

To develop a versatile toolkit of dye-displacement sensors for detecting cationic peptides, specifically histone modifications.
To demonstrate the capability of a chemical sensor array composed of these sensors to robustly discriminate various histone code elements.

Main Methods:

A mix-and-match approach combining readily available dyes and calixarene host molecules to create dye-displacement sensors.
Utilizing a chemical sensor array comprising two or three supramolecular sensors to generate data fingerprints for histone modification analysis.
Employing the sensor array to identify different modifications, combinations of modifications, and sequence contexts on histone tails.

Main Results:

The sensor array successfully discriminated between unmethylated, mono-, di-, and trimethylated lysines on histone tails.
The system identified various modification types and combinations within single histone tail sequences and different sequence contexts.
Isomeric dimethylarginine modifications were also identified, overcoming limitations faced by antibody-based methods.
The array simultaneously reported on the concentrations and identities of histone modifications.

Conclusions:

A novel toolkit of supramolecular sensors enables robust discrimination of diverse histone code elements.
This sensor array offers a powerful and versatile platform for analyzing histone modifications, including challenging targets.
The ability to simultaneously determine concentration and identity advances the study of epigenetic regulation and related diseases.