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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...

Position-effect Variegation

Position-effect Variegation

In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.

The Nucleosome Core Particle

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...

The Nucleosome Core Particle

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...

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Related Experiment Video

Updated: Jun 6, 2026

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Sequence-dependent histone variant positioning signatures.

Ngoc Tu Le¹, Tu Bao Ho, Bich Hai Ho

¹School of Knowledge Science, Japan Advanced Institute of Science and Technology, Nomi, Ishikawa, Japan. ngoctule@jaist.ac.jp

|December 15, 2010

Summary

This summary is machine-generated.

Genomic sequences influence where histone variants like H2A.Z and H3.3 are deposited on DNA. Specific DNA sequences, such as CA/TG dinucleotides, help distinguish target sites for these histone variants.

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Published on: May 17, 2016

Area of Science:

Epigenetics
Molecular Biology
Genomics

Background:

Nucleosomes, composed of DNA and histone proteins, are the basic units of chromatin.
Histone variants possess distinct biochemical properties and biological roles.
Mechanisms governing histone variant deposition onto chromatin remain largely unknown.

Purpose of the Study:

To investigate the role of genomic sequences in directing the deposition of histone variants.
To identify specific DNA sequence motifs associated with different histone variants.

Main Methods:

Analysis of genomic sequences from human nucleosomes containing specific histone variants (H2A.Z, H3.3, and double variants).

Main Results:

Genomic sequence composition partially determines target sites for histone variant deposition.
The dinucleotides CA/TG are critical for differentiating target sites between H2A.Z-only and H3.3-containing nucleosomes.

Conclusions:

A DNA-mediated mechanism regulates the deposition of distinct histone variants.
This finding offers new insights into epigenetic regulation of cellular processes like transcription and replication.