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Related Concept Videos

Histone Modification02:32

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 Modification02:32

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,...
The Nucleosome Core Particle01:12

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 Particle02:10

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...
The Nucleosome01:19

The Nucleosome

Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...
The Nucleosome02:33

The Nucleosome

DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...

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Related Experiment Video

Updated: Jun 17, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

Nickel binding to histone H4.

Maria Antonietta Zoroddu1, Massimiliano Peana, Serenella Medici

  • 1Department of Chemistry & Pharmacy Faculty, University of Sassari, via Vienna 2, 07100, Sassari, Italy. zoroddu@uniss.it

Dalton Transactions (Cambridge, England : 2003)
|January 13, 2010
PubMed
Summary
This summary is machine-generated.

Carcinogenic nickel compounds inhibit histone H4 acetylation by inducing alpha-helical structures. This structural change in histone H4 may disrupt gene regulation and the "histone code".

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Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

Related Experiment Videos

Last Updated: Jun 17, 2026

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Nickel compounds are known carcinogens that interfere with cellular processes.
  • Histone acetylation, particularly of histone H4, plays a crucial role in transcriptional regulation.
  • Acetylation of histone H4's N-terminal tail induces conformational changes, increasing alpha-helical structure.

Purpose of the Study:

  • To investigate the conformational changes induced by carcinogenic nickel compounds on histone H4.
  • To determine if nickel affects histone H4 structure similarly to acetylation.

Main Methods:

  • Circular dichroism spectroscopy was used to study the secondary structure of histone H4 upon interaction with nickel compounds.

Main Results:

  • Nickel compounds were found to induce a significant increase in the alpha-helical conformation of histone H4.
  • This nickel-induced structural change mimics the effect of histone acetylation.
  • The conformational change is proposed to hinder histone acetyl transferase binding and function.

Conclusions:

  • Nickel's ability to induce alpha-helical structures in histone H4 may be a key mechanism in its carcinogenic activity.
  • This disruption of histone H4 structure could compromise the
  • histone code
  • and affect gene expression.