核酸三リン酸塩のRNAポリメラーゼへのアロステリック結合は,転写延長を調節する

J E Foster¹, S F Holmes, D A Erie

¹Department of Chemistry, University of North Carolina, Chapel Hill, NC 27599, USA.

Cell

|August 21, 2001

まとめ

研究者らは,E. coli RNAポリメラーゼに新しいアロステル結合部位を発見した. この部位にテンプレートニュクレオチドが結合すると,酵素が活性化し,転写の延長速度が増加します.

科学分野:

分子生物学は分子生物学である.
バイオケミストリーバイオケミストリー
エンジム・キネティクス

背景:

トランスクリプションの調節には,RNAポリメラーゼの構成状態が含まれます.
これらの状態を制御する要因は完全に理解されていません.
RNAポリメラーゼのダイナミクスを理解することは,遺伝子発現制御に不可欠です.

研究の目的:

RNAポリメラーゼの構成状態を制御する要因を調査する.
ヌクレオチドの組み込み調節のメカニズムを解明する.
RNAポリメラーゼ機能におけるアロステル調節を特定するために.

主な方法:

単一ヌクレオチドの組み込みを研究するためのトランジント状態運動学.
E. coli RNAポリメラーゼの酵素運動分析.
ヌクレオチド結合部位の特徴. ニュクレオチド結合部位の特徴.

主要な成果:

E. coli RNAポリメラーゼは,触媒部位と異なるアロステル結合部位を有しています.
テンプレート核酸三リン酸 (NTP) がアロステル部位に結合すると,核酸の組み込み率が向上する.
ノンテンプレートされたNTPは,アロステリック部位に結合したり,影響したりしません.
RNAポリメラーゼは,遅い (非活性化) と速い (活性化) 触媒状態に存在する.
テンプレートされたNTPをアロステリック部位に結合させることで,非活性状態から活性化状態への移行が誘発されます.

結論:

E. coli RNAポリメラーゼのアロステリックサイトは,転写の延長を調節する.
この部位へのテンプレート NTP 結合は,より迅速な核酸組み込みのための酵素を活性化します.
このメカニズムは,転写中のRNAポリメラーゼの構成動態の制御に関する洞察を提供します.

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