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

Histone Modification02:32

Histone Modification

13.4K
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...
13.4K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

8.3K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
8.3K
Nucleosome Remodeling02:54

Nucleosome Remodeling

9.2K
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...
9.2K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

953
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...
953
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

6.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.9K
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

1.7K
Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
1.7K
このページは機械翻訳されています。他のページは英語で表示される場合があります。View in English
  1. ホーム
  2. 研究分野
  3. 生物学的科学
  4. 遺伝学
  5. エピジェネティクス (ゲノムメチレーションとエピジェノミクスを含む)
  6. 核局所化されたα-ケトグルタレット脱水素酵素によるヒストン脱甲基化の制御

核局所化されたα-ケトグルタレット脱水素酵素によるヒストン脱甲基化の制御

Fei Huang1,2, Xiao Luo2,3, Yang Ou1,2

  • 1National Key Laboratory of Wheat Improvement, Peking-Tsinghua Center for Life Sciences, School of Advanced Agricultural Sciences, Peking University, Beijing 100871, China.

Science (New York, N.Y.)
|July 13, 2023

関連する実験動画

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

7.5K
Analysis of Histone Antibody Specificity with Peptide Microarrays
09:47

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

40.4K
Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

4.0K

PubMed で要約を見る

まとめ
この要約は機械生成です。

酵素α-ケトグルタレート脱水素酶 (KGDH) は,植物における遺伝子発現を制御するジュンジCドメインを含むヒストン脱甲基化酶 (JMJs) によってヒストンの脱甲基化を調節するために核に入ります.

科学分野:

  • 分子生物学
  • エピジェネティクス
  • 植物学

背景:

  • ヒストンのメチル化は,真核転写の調節に不可欠である.
  • Jumonji Cドメインを含むヒストン脱甲基化 (JMJs) はヒストンのメチル化レベルを制御する.
  • 一般的なJMJ活動を規制するメカニズムはほとんど不明です.

研究 の 目的:

  • JMJ活動の規制メカニズムを調査する.
  • α-ケトグルタレット依存ヒストンの脱メチル化を制御する要因を特定する.

主な方法:

  • α-ケトグルタレット脱水素酵素 (KGDH) の核局所化研究
  • アラビドプシス・タリアナのJMJとのKGDH相互作用の分析
  • クロマチンの免疫流出により,KGDHが濃縮された場所が特定される.
  • α-ケトグルタレットのデカルボキシル化とヒストンの脱メチル化を測定する.

主要な成果:

  • KGDHは核に転移し,様々なJMJと相互作用する.
  • 核KGDHはα-ケトグルタレット依存ヒストンの脱メチル化を調節する.
  • KGDHは環境信号によって影響され,数千の位置で濃縮されます.

関連する実験動画

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
10:09

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

7.5K
Analysis of Histone Antibody Specificity with Peptide Microarrays
09:47

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

40.4K
Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

4.0K
  • クロマチン結合のKGDHは,α-ケトグルタレットの可用性を制限し,脱メチル化を阻害する.
  • 結論:

    • JMJ媒介ヒストンの脱メチル化のための新しい調節メカニズムを発見しました.
    • 代謝酵素KGDHが表遺伝子調節に 作用することを示した.
    • 植物における代謝状態と全ゲノムにわたる遺伝子発現制御の関連性を強調した.