人間の一般転写因子 TFIID コア複合体の構造
Christoph Bieniossek1, Gabor Papai, Christiane Schaffitzel
1European Molecular Biology Laboratory Grenoble Outstation, Unit of Virus Host Cell Interactions UVHCI, UJF-CNRS-EMBL Unité Mixte International UMI 3265, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France.
Nature
|January 8, 2013
まとめ
人間のコアTFIIDの構造は,TAF8-TAF10結合時に非対称性へと移行する対称的なアーキテクチャを明らかにし,遺伝子転写調節のためのホロTFIIDアセンブリをガイドします.
科学分野:
- 分子生物学は分子生物学である.
- 構造生物学 構造生物学とは
- 遺伝子規制 遺伝子規制
背景:
- 転写因子IID (TFIID) は,RNAポリメラーゼIIによる遺伝子転写開始に不可欠である.
- TFIIDは,TATA-box-binding protein (TBP) と13のTBP関連因子 (TAF) の大きな複合体である.
- TFIIDの正確なアーキテクチャと組み立て経路は,ほとんど不明のままです.
研究 の 目的:
- 人間のコアの高解像度構造を決定する-TFIID.
- ホロTFIIDの組み立てにおけるコアTFIID対称性の役割を明らかにする.
- TFIIDが遺伝子転写をどのように促進するかを理解する.
主な方法:
- クリオ電子顕微鏡 (cryo-EM) で11.6 Åの解像度.
- 人間のコアの構造分析-TFIID.
- TAF8-TAF10複合体の結合を研究するための生化学分析.
主要な成果:
- 人間のコア-TFIIDの構造は,二重対称で交互に絡み合ったアーキテクチャを示しています.
- ヒストン折りを含むTAFの保存された構造的特徴は,コア-TFIID構造内に収容されています.
- TAF8-TAF10複合体の結合は,コア-TFIIDの対称性を破壊し,非対称な支架を作成します.
結論:
- 非対称なコア-TFIID構造は,ホロ-TFIIDアセンブリのための核化部位として機能します.
- この対称性から非対称性への構造的移行は,TFIIDの組立経路にとって極めて重要です.
- TFIIDの構造を理解することは,遺伝子転写の調節に関する洞察を提供します.
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