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Related Concept Videos

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...
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 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...
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 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 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...

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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 11, 2013

A histone code for chromatin assembly.

Jeffrey Fillingham1, Jack F Greenblatt

  • 1Banting and Best Department of Medical Research, Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada.

Cell
|July 30, 2008
PubMed
Summary
This summary is machine-generated.

Histone H3 lysine 56 acetylation is crucial for chromatin assembly during DNA replication and repair. This modification facilitates histone deposition by specific chaperone proteins, ensuring genome stability.

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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Last Updated: May 11, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 11, 2013

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Histone modifications play critical roles in regulating DNA accessibility and function.
  • Histone H3 lysine 56 (H3K56) acetylation is a recently identified mark with proposed roles in chromatin dynamics.

Purpose of the Study:

  • To investigate the function of histone H3 lysine 56 acetylation in chromatin assembly.
  • To determine the involvement of H3K56 acetylation in DNA replication and repair processes.

Main Methods:

  • Utilizing genetic and biochemical approaches to study histone deposition and chromatin assembly.
  • Employing techniques to analyze the impact of H3K56 acetylation on chromatin structure and function.

Main Results:

  • Acetylation of H3K56 promotes chromatin assembly during the S phase of the cell cycle.
  • Histone chaperones CAF-1 and Rtt106 mediate H3K56 acetylation-dependent histone deposition.
  • The H3K56 acetylation mark facilitates chromatin reassembly after DNA double-strand break repair.

Conclusions:

  • Histone H3 lysine 56 acetylation is a key regulator of chromatin assembly.
  • This acetylation mark is essential for maintaining genome integrity during DNA replication and repair.