Jove
Visualize
お問い合わせ
JoVE
x logofacebook logolinkedin logoyoutube logo
JoVEについて
概要リーダーシップブログJoVEヘルプセンター
著者向け
出版プロセス編集委員会範囲と方針査読よくある質問投稿
図書館員向け
推薦の声購読アクセスリソース図書館諮問委員会よくある質問
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experimentsアーカイブ
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教員リソースセンター教員サイト
利用規約
プライバシーポリシー
ポリシー

関連する概念動画

The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.0K
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...
2.0K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

13.9K
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...
13.9K
The Nucleosome02:33

The Nucleosome

18.2K
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...
18.2K
The Nucleosome01:19

The Nucleosome

3.5K
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...
3.5K
The Nucleosome02:33

The Nucleosome

4.7K
4.7K
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

4.9K
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...
4.9K

こちらも読む

関連記事

共著者、ジャーナル、引用グラフによってこの研究に関連する記事。

並び替え
Same author

Human RNA polymerase III termination favors decomposition over facilitated recycling.

Nature communications·2026
Same author

BCL7A's arginine anchor links nucleosome recognition to chromatin remodeling and diffuse large B-cell lymphoma tumor suppression.

Protein & cell·2026
Same author

Kinetic control of mammalian transcription elongation.

Nature structural & molecular biology·2025
Same author

Dynamic U2AF cycling defines two phases of cotranscriptional pre-mRNA splicing.

Science (New York, N.Y.)·2025
Same author

DSS1 is required for proper Integrator-PP2A function.

Nature communications·2025
Same author

Structural insights into human Pol III transcription initiation in action.

Nature·2025

関連する実験動画

Updated: Dec 29, 2025

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

12.0K

核細胞結合BAF複合体の構造

Shuang He1,2, Zihan Wu1,2, Yuan Tian1,2

  • 1Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering, and Shanghai Key Laboratory of Medical Epigenetics, Shanghai Medical College of Fudan University, Shanghai 200032, China.

Science (New York, N.Y.)
|February 1, 2020
PubMed
まとめ

この研究は,ヒトのBRG1/BRM関連因子 (BAF) コンプレックスが核細胞に結合する構造を明らかにした. クロマチンリモデラー

さらに関連する動画

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 10, 2013

23.0K
Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
08:44

Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes

Published on: October 23, 2014

10.3K

関連する実験動画

Last Updated: Dec 29, 2025

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

12.0K
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 10, 2013

23.0K
Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
08:44

Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes

Published on: October 23, 2014

10.3K

科学分野:

  • 分子生物学
  • 構造生物学
  • 生物化学

背景:

  • BRG1/BRM関連因子 (BAF) とポリブローム関連BAF (PBAF) を含む哺乳類のSWI/SNF複合体は,クロマチンの構造と遺伝子転写の重要な調節因子である.
  • 機能不全のSWI/SNF複合体,特にBAFは,そのサブユニットの変異により,様々なヒトがんに関与しています.
  • BAF-核細胞相互作用の構造的基礎を理解することは,細胞プロセスと疾患におけるその役割を解読するために不可欠です.

研究 の 目的:

  • ヒトのBAF複合体の高解像度構造を明らかにする.
  • BAF複合体のサブユニット組織と核細胞認識メカニズムについての詳細な洞察を提供すること.
  • BAFサブユニットとヌクレオソームの間の重要な相互作用を特定し,特に癌に関連した変異に焦点を当てます.

主な方法:

  • 低温電子顕微鏡 (cryo-EM) を用いて,ヒトBAF核細胞複合体の構造を3. 7アングストームの解像度で決定した.
  • BAFサブユニットと核細胞DNAおよびヒストンの間の相互作用を特徴付けるために生化学的および構造的分析が行われました.

主要な成果:

  • 凍結EM構造は,核細胞がBAF複合体の塩基とアデノシントリフォスファターゼ (ATPase) モジュールの間に位置し,アクチン関連タンパク質 (ARP) モジュールによって接続されていることを示しています.
  • ATPアゼモーターは核細胞DNAの近くに位置し,ATPの水解によって核細胞細胞に沿ってDNAの転位を容易にする.
  • SMARCB1サブユニットのC端のヘリクスは,核細胞の酸性パッチと相互作用し,この領域はがんで頻繁に変異します.
  • AT豊富なインタラクティブドメインを含むタンパク質1A (ARID1A) とSMARCCは,それぞれBAFベースモジュールの構造的コアとエスカフォルドを形成する.

結論:

  • この研究は,ヒトのBAF複合体が核細胞と相互作用する前例のない構造的詳細を提供します.
  • これらの発見は,BAFがクロマチンを再構成するメカニズムを明らかにし,SMARCB1のようなサブユニットにおける癌に関連した変異の構造的重要性を強調しています.
  • 決定された構造は,遺伝子調節におけるBAF機能と腫瘍形成におけるその役割を理解するための基礎として機能する.