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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...

Histone Modification

Histone Modification

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...

Duplication of Chromatin Structure

Duplication of Chromatin Structure

The process of chromosome duplication during cell division requires genome-wide disruption and re-assembly of chromatin. The chromatin structure must be accurately inherited, reassembled, and maintained in the daughter cells to ensure lineage propagation.
The basic unit of the chromatin is the nucleosome, consisting of DNA wrapped around octameric histone proteins and short stretches of linker DNA separating individual nucleosomes. The histone proteins within the nucleosome have their...

Euchromatin

Euchromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...

Inheritance of Chromatin Structures

Inheritance of Chromatin Structures

Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...

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Related Experiment Video

Updated: Nov 21, 2025

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

Transcription shapes genome-wide histone acetylation patterns.

Benjamin J E Martin¹, Julie Brind'Amour², Anastasia Kuzmin¹

¹Department of Biochemistry and Molecular Biology, Life Sciences Institute, Molecular Epigenetics Group, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada.

Nature Communications

|January 12, 2021

Summary

Histone acetylation, a key mark of gene activity, is mostly caused by transcription itself. RNA polymerase II (RNAPII) drives histone acetyltransferases (HATs) to genes, making acetylation a consequence, not a cause, of transcription.

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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

Area of Science:

Molecular Biology
Epigenetics
Gene Regulation

Background:

Histone acetylation is widely recognized as a hallmark of active gene transcription.
The causal relationship between histone acetylation and transcription remains unclear.

Purpose of the Study:

To investigate whether histone acetylation is a cause or consequence of transcription.
To elucidate the mechanisms linking histone acetylation and RNA polymerase II (RNAPII) activity.

Main Methods:

Utilized immunoblotting and chromatin immunoprecipitation-sequencing (ChIP-seq) in Saccharomyces cerevisiae.
Analyzed the genome-wide distribution and dependency of histone acetylation.
Investigated the role of RNAPII and transcription activators in histone acetyltransferase (HAT) recruitment and activity.

Main Results:

The majority of histone acetylation is dependent on active transcription.
RNA polymerase II (RNAPII) is required for the interaction of histone acetyltransferases (HATs) with gene bodies.
Promoter-bound HATs cannot acetylate histones without ongoing transcription, indicating post-recruitment regulation.
Histone acetylation is elevated at nucleosomes that impede RNAPII progression, supporting a model of transcription-dependent acetylation.

Conclusions:

Histone acetylation is primarily a consequence of transcription, not a prerequisite.
RNAPII plays a crucial role in both recruiting and activating HATs within gene bodies.
This study reframes histone acetylation as a downstream event regulated by the transcription machinery.