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Related Concept Videos

The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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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...
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The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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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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Histone Modification02:32

Histone Modification

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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...
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Histone Modification02:32

Histone Modification

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Heterochromatin02:38

Heterochromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at...
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The Nucleosome01:19

The Nucleosome

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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...
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Related Experiment Video

Updated: Mar 11, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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A Molecular Prospective for HIRA Complex Assembly and H3.3-Specific Histone Chaperone Function.

M Daniel Ricketts1, Ronen Marmorstein2

  • 1Department of Biochemistry and Biophysics, Graduate Group in Biochemistry and Molecular Biophysics, Abramson Family Cancer Research Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, PA 19104, USA.

Journal of Molecular Biology
|November 23, 2016
PubMed
Summary

Histone variant H3.3 plays crucial roles in gene regulation and DNA repair. The human histone cell cycle regulator (HIRA) complex facilitates H3.3 deposition, with new models explaining its assembly and function.

Keywords:
CABIN1HIRAUBN1histone H3.3histone chaperones

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Histone variants and post-translational modifications regulate chromatin structure and function.
  • Histone H3.3, distinct from H3.1, influences gene transcription, heterochromatin formation, and DNA repair.
  • The HIRA complex is a key chaperone for H3.3/H4 deposition into chromatin.

Purpose of the Study:

  • To review existing data on the HIRA complex.
  • To present a novel model for HIRA complex assembly.
  • To elucidate the mechanism of HIRA-mediated H3.3/H4 chromatin incorporation.

Main Methods:

  • Review of biochemical and structural studies.
  • Analysis of protein-protein interactions within the HIRA complex.
  • Modeling of HIRA complex assembly and function.

Main Results:

  • The HIRA complex comprises HIRA, ubinuclein-1, CABIN1, and anti-silencing function 1.
  • Recent studies provide insights into the assembly and function of this H3.3-specific chaperone.
  • A new model for HIRA complex assembly and H3.3/H4 deposition is proposed.

Conclusions:

  • The HIRA complex is essential for depositing the H3.3 histone variant.
  • Understanding HIRA complex dynamics is crucial for comprehending chromatin regulation.
  • The proposed model offers a framework for future research into H3.3-mediated epigenetic processes.