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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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Updated: May 11, 2026

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

クロマチンアセンブリのためのヒストンコード.

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
まとめ
この要約は機械生成です。

ヒストンH3ライシン56アセチル化は,DNA複製と修復の間にクロマチンの組み立てに不可欠です. この改変は,特定のチャペロンタンパク質によるヒストンの堆積を促進し,ゲノム安定性を確保します.

さらに関連する動画

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

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

関連する実験動画

Last Updated: May 11, 2026

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

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

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

科学分野:

  • 分子生物学は分子生物学である.
  • エピジェネティクス エピジェネティクス
  • クロマチン生物学 クロマチン生物学

背景:

  • ヒストンの改変は,DNAのアクセシビリティと機能を調節する上で重要な役割を果たします.
  • ヒストンH3リジン56 (H3K56) アセチル化は,クロマチンのダイナミクスにおける役割が提案されている,最近特定されたマークです.

研究 の 目的:

  • クロマチンアセンブリにおけるヒストンH3リジン56アセチル化の機能を調査する.
  • DNA複製および修復プロセスにおけるH3K56アセチル化の関与を決定する.

主な方法:

  • 遺伝学および生化学的アプローチを用いてヒストンの堆積とクロマチンの組成を研究する.
  • H3K56アセチル化がクロマチンの構造と機能に与える影響を分析する技術を用いる.

主要な成果:

  • H3K56のアセチル化により,細胞周期のS段階においてクロマチンの組み立てが促進されます.
  • ヒストンのチャペロンであるCAF-1とRtt106は,H3K56のアセチル化依存ヒストンの堆積を媒介する.
  • H3K56アセチル化マークは,DNA二重鎖の断裂修復後にクロマチンの再組みを容易にする.

結論:

  • ヒストンH3ライシン56アセチル化は,染色体組成の重要な調節因子である.
  • このアセチル化マークは,DNA複製と修復の間にゲノムの完全性を維持するために不可欠です.