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Purification of Hsp104, a Protein Disaggregase

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酵母Hsp110 Sse1の結晶構造から,Hsp70チャペロン活性に関する洞察

Qinglian Liu¹, Wayne A Hendrickson

¹Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

|October 10, 2007

まとめ

熱ショックタンパク質110s (Hsp110s) は,構造分析により,Hsp70の近親であることが明らかになった. この発見は,Hsp70スーパーファミリー内の進化的リンクとアロステリックメカニズムを明確にします.

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:

熱ショックタンパク質 (HSP) は,タンパク質のホメオスタシスにとって極めて重要です.
Hsp70のシャペロンはよく研究されているが,Hsp110は遠い親戚と考えられていた.
Hsp110の構造と機能を理解することは,Hsp70超家族進化の鍵です.

研究の目的:

Hsp110sとHsp70sの構造的関係を決定する.
Hsp70の機能を制御するアロステリックメカニズムを解明する.
Hsp110s.の進化的起源を調査する.

主な方法:

ATPによるSse1 (Hsp110) の2.4A解像度構造を決定するX線結晶学.
Hsp110とHsp70ドメインの比較構造分析.
Sse1 と Hsp70 ホモログの64の変異変異体の機能分析.

主要な成果:

Sse1 (ATP) の構造は,Hsp110sがHsp70の近親であることを示している.
Sse1ドメイン間の広範囲で保存されたインターフェースは,Hsp70sを反映しています.
Sse1 (ATP) ドメインとHsp70 ドメインの構成の違いは,進化的なつながりを示唆しています.

結論:

Hsp110sは,Hsp70sの進化的に保存された親戚であり,祖先のHsp70のATP状態を潜在的に表しています.
この研究は,Hsp70s.内のアロステリック通信に関する原子レベルの洞察を提供します.
Hsp110sは,酵母生存に不可欠な核酸交換因子として明確に機能します.

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