T複合ポリペプチド-1は,真核細胞細胞溶液内の異体粒子のサブユニットです
V A Lewis1, G M Hynes, D Zheng
1Institute of Cancer Research, Chester Beatty Laboratories, London, UK.
Nature
|July 16, 1992
まとめ
T複合ポリペプチド-1 (TCP1) は,ユニークなヘテロオリゴメリック粒子に含まれる細胞性タンパク質です. この粒子は,この粒子です.
科学分野:
- 分子生物学は分子生物学である.
- 細胞生物学 細胞生物学
- バイオケミストリー バイオケミストリー
背景:
- T複合体ポリペプチド-1 (TCP1) は,ネズミのt複合体によって暗号化され,ほとんどの細胞で発現し,特に精子生成中に上昇調節されます.
- 哺乳類のTCP1配列は,相互に高い同一性 (>96%) を示し,酵母とドロソフィラのオートロゴーと有意な同一性 (>60%) を示し,機能が保存されていることを示唆しています.
- TCP1は酵母に欠かせないもので,哺乳類の細胞溶液に相当する,分子チャペロンであるgroELであると考えられている.
研究 の 目的:
- ヒトとネズミのTCP1の原生構造と組成を特徴づけること.
- 細胞性タンパク質の折りたたみ機構としてのTCP1の潜在的な役割を調査する.
主な方法:
- 負染色電子顕微鏡を用いて,TCP1粒子の構造特性を決定した.
- 生化学分析は,ネイティブTCP1複合体内の関連タンパク質を特定するために使用されました.
主要な成果:
- マウリンとヒトのTCP1は,サイトソール内の大きなヘテロオリゴメリック粒子 (800K-950K) として存在します.
- この粒子は4〜6つの未確認のタンパク質と2つのHsp70熱ショックタンパク質と関連しています.
- 電子顕微鏡では,直径12〜16nmの2つの積み重ねられたリングのユニークな構造を明らかにしました.
結論:
- TCP1は,チャペロニン60タンパク質との類似性にもかかわらず,生化学的および構造的に異なっている.
- TCP1は,タンパク質の折りたたみに関与する新種のユーカリ細胞性分子ファミリーの一部である可能性があります.
- ヘテロメア結合は,TCP1の機能を調節する役割を果たす可能性が高い.
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