転写共活性化剤p300とCBPはヒストンアセチルトランスファーゼである
V V Ogryzko1, R L Schiltz, V Russanova
1Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-2753, USA.
Cell
|November 29, 1996
まとめ
p300/CBPタンパク質は新しいヒストンアセチルトランスフェラーゼとして作用し,核細胞内のコアヒストンを改変します. この発見は,遺伝子調節に関与するアセチルトランスファーゼの新種を明らかにしています.
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
- 遺伝子規制 遺伝子規制
背景:
- p300/CBPはトランスクリプションアダプタとして機能し,アクティベーターからの信号を統合します.
- 細胞およびウイルス要因はp300/CBPを標的とし,転写と細胞周期に影響を与える.
- PCAFはp300/CBP関連因子であり,ヒストンアセチルトランスフェラーゼの内在的な活性を持っています.
研究 の 目的:
- p300/CBPの酵素活性について調べる.
- p300/CBPがヒストンアセチルトランスファーゼ (HAT) 活性を持つかどうかを判断する.
- p300/CBP.によって表されるアセチルトランスフェラーゼの新種を特徴づける.
主な方法:
- タンパク質の相互作用を評価するための生化学的測定法.
- 酵素活性アッセイはヒストンのアセチル化を測定する.
- アセチルトランスファーゼにおける保存モチーフの分析.
主要な成果:
- p300/CBPはヒストンアセチルトランスフェラーゼ活性を示しています.
- p300/CBPは,核細胞内の4つの核ヒストンをすべてアセチル化します.
- p300/CBPには,他のアセチルトランスフェラーゼに特有の保存モチーフが欠け,新しいクラスであることを示しています.
結論:
- p300/CBPはヒストンアセチルトランスフェラーゼの新型であり,以前に特徴づけられた酵素とは異なる.
- p300/CBPは,PCAFと併用してアセチレート核細胞を発生させる可能性が高い.
- これらの発見は,表遺伝的調節と転写制御の理解を広げています.
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