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チャペロニンのTRiC/CCTは,細胞のプロテオスタシスに不可欠な保存された静電界面を通して,プレフォルディンと結合する

Daniel Gestaut¹, Soung Hun Roh², Boxue Ma³

¹Department of Biology and Genetics, Stanford University, Stanford, CA 94305, USA.

|April 9, 2019

まとめ

主要なチャペロンであるTRiC/CCTとプレフォルディン/GIMc (PFD) は,タンパク質の折り畳みに不可欠な超チャペロン組成を形成する. この複合体は有毒なタンパク質の蓄積を防止し,細胞のプロテオスタシスを維持します.

科学分野:

分子生物学
構造生物学
細胞生物学

背景:

ユーカリオットタンパク質の折り畳みは,TRiC/CCTとプレフォルディン/GIMc (PFD) のようなチャペロンシステムに依存しています.
プロテオスタシスを維持するためにこれらのチャペロン間の協力を理解することは不可欠です.

研究の目的:

TRiC/CCTとPFDの構造的・機能的相互作用を明らかにする.
PFDがTRiC/CCTのタンパク質折り畳み活動を強化するメカニズムを調査する.

主な方法:

クリオ電子顕微鏡 (cryo-EM) で,TRiC-PFD複合体の構造を決定する.
タンパク質とタンパク質の相互作用をマッピングするクロスリンクング質量スペクトロメトリー
機能的影響を評価するために生化学および細胞測定.

主要な成果:

TRiC/CCTとPFDは,保存された静電界面を通じて結合し,定義されたアーキテクチャを形成します.
PFDは,開いた状態と閉じた状態の間の構成サイクルを示し,基板結合室を並べます.
PFDはTRiC/CCTの折り畳み率と収穫量を高め,非生産的なサイクルを抑制します.
TRiC- PFDの相互作用が妨げられれば,アミロイドの蓄積が体内で行われる.

結論:

TRiC-PFDのスプラチャペロン組は,効果的な細胞プロテオスタシスに不可欠です.
この複合体は有毒なタンパク質の形状を防ぎタンパク質の折りたたみ性を維持します
相互作用は細胞の健康に不可欠であり,その障害は有害な影響を及ぼします.

キーワード:

CCT について GIMc トリックス XL-MS について付き添いチャペロニンクリオ・エムプリフォルディンプロテオスタシス

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