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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
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ミトコンドリアの熱ショックタンパク質 hsp60 は,酵母ミトコンドリアに輸入されたタンパク質の組み立てに不可欠です
M Y Cheng1, F U Hartl, J Martin
1Yale University School of Medicine, Department of Human Genetics, New Haven, Connecticut 06510.
Nature
|February 16, 1989
まとめ
核でコードされたミトコンドリア熱ショックタンパク質60 (hsp60) は,輸入タンパク質をミトコンドリアマトリックス複合体に組み立てるのに不可欠です. このチャペロニンタンパク質は,ミトコンドリア内のタンパク質の折り畳みと複合体の形成を促進します.
科学分野:
- ミトコンドリア生物学 ミトコンドリア生物学
- 分子チャペロンは,分子チャペロンを伴います.
- タンパク質のホメオスタシス
背景:
- ミトコンドリアのタンパク質は,核で合成され,マトリックスに輸入されます.
- 適切な折り畳みと組み立ては,タンパク質の機能に不可欠です.
- 熱ショックタンパク質は,細胞のストレス反応とタンパク質の折りたたみにおいて重要な役割を果たします.
研究 の 目的:
- タンパク質の輸入と組み立てにおける核コード化されたミトコンドリア熱ショックタンパク質60 (hsp60) の役割を調査する.
- チャペロニンタンパク質ファミリーのメンバーとしてhsp60を特徴付ける.
主な方法:
- ミトコンドリアへのタンパク質輸入の分析.
- hsp60のオリゴメリック状態の特徴.
- E. coli GroEL.のような既知のチャペロニンとの比較.
主要な成果:
- 核でコードされたhsp60は,ミトコンドリアマトリックス内のオリゴメリック複合体への輸入タンパク質の組み立てに不可欠です.
- hsp60は分子チャペロンとして機能し,タンパク質の折りたたみと組み立てを促進します.
- hsp60は,チャペロニン級のタンパク質に属しています.
結論:
- ミトコンドリア hsp60は,ミトコンドリアマトリックス内のタンパク質の正しい組み立てに不可欠です.
- hsp60のチャペロニン活動は,ミトコンドリアタンパク質のホメオスタシスの維持に不可欠です.
- hsp60は,他のチャペロニンと機能的,構造的類似性を共有し,タンパク質の折りたたみにおける保存されたメカニズムを強調しています.
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Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Generally, polypeptides are unfolded by two distinct...
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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