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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,...

Histone Variants at the Centromere

Histone Variants at the Centromere

Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...

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: Jun 2, 2026

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

Revealing histone variant induced changes via quantitative proteomics.

Anna M Arnaudo¹, Rosalynn C Molden, Benjamin A Garcia

¹Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.

Critical Reviews in Biochemistry and Molecular Biology

|April 30, 2011

Summary

Histone variants, crucial for chromatin complexity, are challenging to analyze with traditional methods. Mass spectrometry-based proteomics offers advanced techniques for their identification and quantification.

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Last Updated: Jun 2, 2026

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Area of Science:

Molecular Biology
Proteomics
Epigenetics

Background:

Histone variants are protein isoforms impacting chromatin architecture.
They play roles in transcription, DNA damage response, and cell cycle regulation.
Distinct sequences and modifications increase biological complexity.

Purpose of the Study:

To review the biology of histone variants.
To discuss mass spectrometry-based proteomics for histone variant characterization.

Main Methods:

Mass spectrometry (MS) techniques for whole protein analysis.
MS techniques for peptide-level analysis.
Review of existing literature on histone variant characterization.

Main Results:

Traditional immunoassay methods face challenges in analyzing histone variants.
Mass spectrometry enables identification and quantification of histone variants.
Proteomics approaches provide detailed characterization.

Conclusions:

Mass spectrometry-based proteomics is a powerful tool for studying histone variants.
These methods overcome limitations of traditional analyses.
Understanding histone variants is key to deciphering chromatin regulation.