関連する実験動画
Updated: Jun 14, 2026
11:19
Genome-wide Analysis using ChIP to Identify Isoform-specific Gene Targets
Published on: July 8, 2010
JARID2およびAEBP2は,H2AK119ub1および他のヒストンの改変の存在下でPRC2を調節する
Vignesh Kasinath1, Curtis Beck2, Paul Sauer3,4
1QB3 Institute, Department of Molecular and Cell Biology, University of California, Berkeley, CA, USA. enogales@lbl.gov vigneshk@berkeley.edu.
Science (New York, N.Y.)
|January 22, 2021
まとめ
ポリコンブ抑制複合体 (PRC1とPRC2) は細胞同一性を調節する. 新しい冷凍EM構造は,JARID2とAEBP2がPRC2をH2AK119ub1に勧誘し,抑制ヒストンのマークを克服する方法を明らかにしています.
科学分野:
- エピジェネティクス
- 分子生物学
- 構造生物学
背景:
- ポリコンブ抑制複合体1と2 (PRC1とPRC2) は,細胞同一性の重要な表遺伝子調節体である.
- PRC1媒介のH2AK119ub1によるPRC2の募集メカニズムは十分に理解されていません.
研究 の 目的:
- コファクターJARID2とAEBP2によるH2AK119ub1へのPRC2の採用の構造的根拠を解明する.
- これらのコファクターが他のヒストンの改変に反応してPRC2の活性を調節する方法を理解する.
主な方法:
- PRC2の冷凍電子顕微鏡 (cryo-EM) 構造の決定は,JARID2,AEBP2,および改変されたヌクレオソームを用いた.
- PRC2活動のコファクター媒介刺激を評価する生化学的測定法
主要な成果:
- 高解像度の冷凍EM構造は,JARID2とAEBP2がH2AK119ub1核細胞と結合し,PRC2と相互作用することを明らかにした.
- JARID2は,EEDとH2AK119-ubiquitinとの相互作用によってPRC2の活性を直接刺激する.
- AEBP2は支架として作用し,その存在はJARID2とともに,H3K4me3とH3K36me3による抑制を部分的に緩和する.
結論:
- JARID2とAEBP2は,ヒストンの改変とPRC2の機能の間のクロストークの重要な媒介です.
- これらのコファクターは,PRC2を標的とし,適切な表遺伝子遺伝子調節と細胞同一性決定のためにその活動を調節する上で重要な役割を果たします.
関連する概念動画
02:04Covalently Linked Protein Regulators
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.
These groups modify specific amino acids in a protein.
02:32Histone 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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:25Spreading of Chromatin Modifications
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 is an enzyme that can...
Writers
The writer is an enzyme that can...
02:30Histone Variants at the Centromere
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 variants are also...
02:04Covalently Linked Protein Regulators
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.
These groups modify specific amino acids in a protein.
02:32Histone 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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...