関連する実験動画
Updated: May 12, 2026

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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
Published on: July 25, 2019
ユビキチン型タンパク質の起源と機能
1Yale University, Department of Molecular Biophysics & Biochemistry, 266 Whitney Avenue, PO Box 208114, New Haven, Connecticut 06520, USA. mark.hochstrasser@yale.edu
Nature
|March 28, 2009
まとめ
ウビキチン型タンパク質 (UBL) は,真核タンパク質を改変し,細胞の重要なプロセスを制御する. 証拠によると,UBL結合はエウカリオートより前に進化し,プロカリオート系から発生した.
科学分野:
- 分子生物学は分子生物学である.
- バイオケミストリー バイオケミストリー
- 進化生物学の進化生物学について
背景:
- ユビキチンとユビキチン型のタンパク質 (UBL) の結合など,エウカリオットタンパク質に変化が起こります.
- UBLは,プロテアソームとクロマチンの採用とのタンパク質の相互作用を含む重要な生理学的プロセスを調節します.
- これらの変化はしばしば一時的なもので,特定の酵素系によって媒介される.
研究 の 目的:
- UBL-タンパク質結合システムの進化的起源を探求する.
- UBL改変経路の潜在的プロカリオット祖先を調査する.
- UBLの結合がユカリオットの出現より前のものであるかどうかを判断する.
主な方法:
- タンパク質改変システムの比較分析.
- UBLの結合と脱結合に関与する酵素ファミリーの検査.
- タンパク質の配列と進化の関係に関するバイオ情報分析.
主要な成果:
- UBL-タンパク質の改変は,真核生物における広範な規制メカニズムである.
- 証拠は,UBLシステムとプロカリオット硫黄転移酵素システムとの間のリンクを示しています.
- UBL結合酵素と解結合酵素に同質なタンパク質は,真核生物の最後の共通の祖先に存在していた.
結論:
- UBL-タンパク質結合は,おそらくプロカリオット系から進化した.
- UBL結合の基本的メカニズムは,真核生物の進化より前のものです.
- UBLの改変は,進化の深い根源を持つ古代の生物学的プロセスです.
関連する概念動画
Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The Proteasome
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Regulated Protein Degradation
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
The Proteasome
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Regulated Protein Degradation
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
The Proteasome
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

