MarR型調節器 AbfRのレドックスセンシングメカニズムに関する構造的洞察
Guijie Liu1,2, Xing Liu1,3, Hongjiao Xu1,2
1Laboratory of Chemical Biology, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203, China.
Journal of the American Chemical Society
|January 15, 2017
まとめ
Staphylococcus epidermidis AbfRによる酸化ストレス調節にはシステインの修正が含まれています. リバーシブルな二酸化物結合は 過剰酸化ではなく DNA結合を阻害し 新しい酸化還元感知機構を明らかにします
科学分野:
- 微生物学
- 構造生物学
- 生物化学
背景:
- AbfRは,Staphylococcus epidermidisのマースター・レドックス感知型転写レギュラータである.
- 酸化ストレス反応と毒性の調節に重要な役割を果たします.
研究 の 目的:
- 様々な酸化状態におけるAbfRのDNA結合メカニズムを解明する.
- AbfRの酸化還元調節の構造的基礎を理解する.
主な方法:
- 還元されたAbfR/DNA複合体,過酸化されたAbfR/DNA,および2硫化物交絡されたAbfR二酸化物に関するX線結晶学.
- 生化学分析について
主要な成果:
- 逆戻り可能な二酸化物改変は,逆戻りできない過酸化とは異なり,AbfRのDNA結合能力を著しく低下させる.
- 1 - ディスルフィードと2 - ディスルフィードの両方のクロスリンクされたAbfRジメルは生物学的に関連しています.
- 過剰酸化されたAbfRはDNA結合を維持するが,生物学的に有意ではない.
- 1-二硫化クロスリンクはDNA結合を弱め,2-二硫化クロスリンクは,DNA結合と相容れない開かれた形状を生成する.
結論:
- AbfRの酸化還元調節には,二硫化結合と過剰酸化がDNA結合に与える差異的な影響を含む新しい特徴が含まれています.
- システインの簡潔な酸化化学は,AbfRにおける効率的な酸化ストレス感知と反応を可能にします.
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