タンパク質ドメインの再結合は,同翻訳的折りたたみによって促進され,真核生物で再結合される
1Cellular Biochemistry & Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
Nature
|July 24, 1997
まとめ
排列タンパク質ドメインの折り畳みは,真核生物の複雑なゲノム進化を助長する. これはバクテリアの折りたたみと対照的に,誤った折りたたみを防止し,新しいタンパク質構造を可能にします.
科学分野:
- 分子生物学は分子生物学である.
- 進化生物学の進化生物学について
- ゲノミクスゲノミクスとは
背景:
- 複雑なゲノムは,タンパク質ドメインの新しい組み合わせによって進化する.
- このプロセスには,モジュール型のポリペプチドにタンパク質の折りたたみが不可欠です.
研究 の 目的:
- ユカリオットとバクテリアの2ドメインポリペプチドの折り畳みメカニズムを調査する.
- モジュラータンパク質の進化における折り畳みの役割を理解する.
主な方法:
- 翻訳中のポリペプチドの折り畳みの比較分析. ユカリオットとEscherichia coliのモデル.
- 連続的,共同翻訳的,および翻訳後の折り畳み経路の検討.
主要な成果:
- ユカリオット翻訳は,2ドメインのポリペプチドの効率的な順序的および共同翻訳的折り畳みを容易にする.
- Escherichia coliは翻訳後の折りたたみを示し,同時に折りたたむドメインの分子内誤折りにつながります.
結論:
- ユカリオットにおける連続ドメインの折り畳みは,モジュール型ポリペプチドの進化に決定的かもしれない.
- このプロセスは,遺伝子融合が機能的なタンパク質構造を生成する可能性を高めます.
関連する概念動画
Protein Folding
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Protein Folding
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Conservation of Protein Domains Over Different Proteins
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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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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Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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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.
The...
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