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

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...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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 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...

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

Elongin B orchestrates chromatin and transcriptional programs in H3K27M-mutant diffuse midline glioma.

bioRxiv : the preprint server for biology·2026
Same author

Expanding the Global Map of Protein Post-Translational Modifications With Immunoaffinity Enrichment and nDIA Analysis on the Orbitrap Astral Mass Spectrometer.

Molecular & cellular proteomics : MCP·2026
Same author

SAGA/ATAC complexes sustain aberrant chromatin regulation and promote tumorigenesis in diffuse midline glioma.

bioRxiv : the preprint server for biology·2026
Same author

Site-specific quantification of the in vivo UFMylome reveals myosin modification in ALS.

Cell reports methods·2025
Same author

An E2 ubiquitin-conjugating enzyme links diubiquitinated H2B to H3K27M oncohistone function.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Metabolic Control of Glycosylation Forms for Establishing Glycan-Dependent Protein Interaction Networks.

bioRxiv : the preprint server for biology·2024
Same journal

A viral ORFeome library for systems-level genetic dissection of host-pathogen interactions.

Cell·2026
Same journal

Co-option of lysosomal machinery shapes the evolution of the intracellular photosymbiosis supporting coral reefs.

Cell·2026
Same journal

LEF1 and niche factors determine T cell stemness across chronic diseases.

Cell·2026
Same journal

Recurrent patterns of TOP1-mediated neuronal genomic damage shared by major neurodegenerative disorders.

Cell·2026
Same journal

Four-dimensional molecular mapping from a spatial snapshot reveals the dynamics of hair follicle organogenesis.

Cell·2026
Same journal

Whole-cell particle-based digital twin simulations from 4D lattice light-sheet microscopy data.

Cell·2026
関連記事をすべて見る

関連する実験動画

Updated: May 18, 2026

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

非対称的に改変された核分裂体.

Philipp Voigt1, Gary LeRoy, William J Drury

  • 1Howard Hughes Medical Institute, New York University School of Medicine, Department of Biochemistry, New York, NY 10016, USA.

Cell
|October 2, 2012
PubMed
まとめ
この要約は機械生成です。

核細胞は,ヒストンのコピーで対称または非対称に変更することができます. この非対称性は遺伝子調節とクロマチンの状態に影響を与え,表遺伝的メカニズムに関する新しい洞察を明らかにします.

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

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

関連する実験動画

Last Updated: May 18, 2026

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

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

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

科学分野:

  • エピジェネティクスと分子生物学
  • クロマチンの生物学
  • 遺伝子規制 遺伝子規制

背景:

  • モノヌクレオソームは,クロマチンの基本単位であり,コアヒストンで構成されており,それらの翻訳後の改変はクロマチンに依存するプロセスにとって極めて重要です.
  • ニュクレオソーム内の個々のヒストンのコピーの正確な in vivo 変異状態は,大部分が未決定のままである.

研究 の 目的:

  • 核細胞内のヒストンのコピーが,in vivoで同等に変化しているかどうかを調査する.
  • シンメトリック対非シンメトリックヒストンの改変の機能的影響を調査する.

主な方法:

  • 胚性幹細胞,線維芽細胞,がん細胞からの核細胞の分析.
  • ヒストンH3ライシン27ディ/トリメチル化 (H3K27me2/3) とH4K20me1.3を検出するテクニックを使用.
  • 直接的な物理的証拠を用いて,H3K4me3,H3K36me3,H3K27me3を含む二価ヒストンの改変を調査する.

主要な成果:

  • 核個体は,H3K27me2/3およびH4K20me1.3の対称的および非対称的に改変された集団の両方を表しています.
  • 対立するH3尾に異なる変異 (H3K4me3/H3K36me3およびH3K27me3) を有する二価核細胞の直接的な証拠が見つかりました.
  • 標的遺伝子のバイバル性は,胚性幹細胞の分化時に解消された.
  • ポリコンブ抑制複合体2媒介のH3K27メチレーションは,対称的に配置されたH3K4me3またはH3K36me3によって抑制されたが,非対称的な配置によって抑制されなかった.

結論:

  • 非対称なヒストンの改変は,多様な機能的な核細胞体の状態を確立する可能性があります.
  • ヌクレオソームに二価特性を組み込むためのメカニズムが提案されています.
  • ヒストン変異非対称性は,遺伝子発現とクロマチンの機能を調節する役割を果たします.