アルギニンリン酸化は,Clpプロテアゼによって分解されるタンパク質を標識する

Débora Broch Trentini¹, Marcin Józef Suskiewicz¹, Alexander Heuck¹

¹Research Institute of Molecular Pathology (IMP), Dr-Bohr-Gasse 7, 1030 Vienna, Austria.

Nature

|November 4, 2016

まとめ

研究者らは,ClpC-ClpPプロテアゼ複合体によって分解される細菌のタンパク質にフォスフォアルギニンがタグ付けされていることを発見しました. この細菌系はユビキチン-プロテアソーム系と類似している.

科学分野:

細菌によるタンパク質分解
プロテアゼ機能
翻訳後の修正

背景:

タンパク質の循環は細胞の健康と信号伝達に不可欠です
ユーカリオットのタンパク質の分解は,ユビキチンタギングに依存しています.
バクテリアのClpプロテアゼの一般的なタグ付けシステムは以前は知られていなかった.

研究の目的:

バチルス・サブティリスのClpC-ClpPタンパク質複合体の標的化メカニズムを解明する.
バクテリアのClpプロテアゼの分解タグを識別する.

主な方法:

ClpPを捕まえる変異体を使った定量的親和プロテオミクス
実験室での解消実験
高解像度の共結晶構造の決定

主要な成果:

アルギニン残基でリン酸化されるタンパク質は,選択的にClpC-ClpPを標的とする.
McsBキナーゼによるアルギニンリン酸化は,基板の分解に必要で十分である.
ClpC ATPaseのフォスフォアルギニンドッキング部位は構造的に解消された.

結論:

フォスフォアルギニンはClpC-ClpPプロテアゼの分解タグとして作用する.
このフォスフォアルギニンのタグ付けシステムは,グラム陽性細菌に保存されます.
このシステムは,ユビキチン-プロテアソーム系と機能的に類似している.

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