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バクテリアのRNAポリメラーゼの結晶構造は,転写阻害タンパク質と結合する
Shunsuke Tagami1, Shun-Ichi Sekine, Thirumananseri Kumarevel
1Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Nature
|December 3, 2010
まとめ
グレー因子ホモログ1 (Gfh1) は,核酸トライホスファートのRNAポリメラーゼ (RNAP) への侵入を阻害することによって転写を阻害する. この結合はRNAPを別の構造状態にロックし,遺伝子発現を防ぐ.
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
- バイオケミストリー バイオケミストリー
背景:
- DNA依存型RNAポリメラーゼ (RNAP) は遺伝子発現に不可欠であり,転写因子によって調節される.
- Thermus属のグレー因子ホモログ1 (Gfh1) は,RNAPに結合することによって転写を阻害する.
- Gfh1媒介による転写抑制の構造的メカニズムは以前は知られていなかった.
研究 の 目的:
- Gfh1.1による転写抑制の構造的基礎を解明する.
- Thermus thermophilus RNAP-Gfh1複合体の構造を決定するために.
主な方法:
- X線結晶グラフィーです.
- RNAP-Gfh1複合体の構造分析
主要な成果:
- Gfh1のアミノ末端のコイルドコイルドメインは,RNAPにおける核酸トリホスファート (NTP) 入口チャネルを阻害する.
- Gfh1は,NTP β-γリン酸結合部位に位置する.
- RNAPは,Gfh1結合によって誘発される,拡張されたチャネルと歪んだブリッジヘリックスを持つ"ラッチ状態"を採用します.
結論:
- Gfh1は,NTP結合を防止し,代替RNAP構成を安定させることで転写を阻害する.
- "ラッチェット状態"はRNAPの転位と転写終了にも影響を与える可能性があります.
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