マルチサイトリン酸化前のおよび後の内在的に乱れたタンパク質の構成特性の配列決定因子

Erik W Martin¹, Alex S Holehouse², Christy R Grace¹

¹Department of Structural Biology, St. Jude Children's Research Hospital , 263 Danny Thomas Place, Memphis, Tennessee 38105, United States.

Journal of the American Chemical Society

|November 4, 2016

まとめ

細胞シグナル伝達における内在的に乱れたタンパク質領域 (IDR) は,マルチサイトリン酸化後でも柔軟なままである. 生物学的研究では,リン酸化はAsh1 IDRを変化させないことが示されています.

科学分野:

生物化学
分子生物学
バイオ物理学

背景:

細胞のシグナリングは本質的に乱れたタンパク質領域 (IDR) に依存する.
マルチサイトリン酸化はIDR機能を調節する.
IDRの形状の変化は,その生物学的役割にとって極めて重要です.

研究の目的:

アッシュ1 本質的に無秩序な領域 (IDR) の構成特性を定量化する.
Ash1 IDRの形状に多部位リン酸化が与える影響を調査する.
IDRコンフォメーションダイナミクスと相関する.

主な方法:

生物物理学的研究
分子シミュレーション
配列パターンの分析

主要な成果:

非酸化アッシュ1 IDRは,膨張したコイル状の形状を示しています.
アッシュ1のマルチサイトリン酸化は,全体的な形状特性を変化させない.
形状の変化は,プロリンと充電された残留物の影響による補償的な局所および遠距離接触によって説明される.

結論:

Ash1 IDRの形状は,配列に依存する補償効果のために,マルチサイトリン酸化には敏感ではありません.
Ash1 IDRの振る舞いを支配する配列の特徴は,他のマルチサイトリン酸化IDRに適用される可能性があります.
研究結果は,細胞信号伝達経路におけるIDRの調節に関する洞察を提供します.

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