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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: Jun 24, 2026

Assays for Validating Histone Acetyltransferase Inhibitors

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Assays for histone deacetylases.

Alexander-Thomas Hauser¹, Mira Jung, Manfred Jung

¹Institute of Pharmaceutical Sciences, University of Freiburg, Freiburg, Germany.

Current Topics in Medicinal Chemistry

|April 10, 2009

Summary

This summary is machine-generated.

Epigenetics involves gene expression changes without altering DNA. Monitoring histone deacetylase (HDAC) activity is crucial for developing new cancer drugs, with in-vitro and cellular assays aiding discovery.

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Area of Science:

Epigenetics and Molecular Biology
Cancer Pathogenesis
Drug Discovery

Background:

Epigenetics governs heritable gene expression changes, impacting development and diseases like cancer.
Histone deacetylases (HDACs) are key epigenetic regulators, particularly in tumor suppressor gene silencing.
HDAC inhibitors represent a promising therapeutic strategy, with vorinostat already approved for cancer treatment.

Purpose of the Study:

To review strategies and protocols for monitoring histone deacetylase (HDAC) activity.
To highlight the importance of HDAC activity monitoring in the development of novel HDAC inhibitors.
To present biochemical in-vitro assays and cellular models for HDAC inhibitor discovery.

Main Methods:

Focus on biochemical in-vitro assays for measuring HDAC activity.
Inclusion of cellular models for validating potential drug candidates (hit validation).
Review of established and emerging methodologies for HDAC activity assessment.

Main Results:

Established in-vitro assays provide robust methods for quantifying HDAC activity.
Cellular models allow for the assessment of HDAC inhibitor efficacy in a biological context.
A comprehensive overview of current monitoring strategies facilitates drug discovery.

Conclusions:

Accurate monitoring of HDAC activity is essential for the rational design of HDAC inhibitors.
A combination of in-vitro and cellular assays offers a powerful approach for drug discovery.
Continued development of monitoring techniques will accelerate the identification of new epigenetic therapies for cancer.