関連する実験動画
Updated: May 8, 2026

08:33
Ubiquitin Chain Analysis by Parallel Reaction Monitoring
Published on: June 17, 2020
単一のサブユニットE2による結合特異的なユビキチン鎖の延長メカニズム
Katherine E Wickliffe1, Sonja Lorenz, David E Wemmer
1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.
Cell
|March 8, 2011
まとめ
Ube2SのようなウビキチンE2酵素は,ウビキチンドナーを指向するために非共性相互作用を使用して,特定のK11鎖の組み立てを可能にします. この基板補助触媒機構は,ユビキチン鎖のトポロジーの調節に極めて重要です.
科学分野:
- バイオケミストリー バイオケミストリー
- 分子生物学は分子生物学である.
- セルラー・シグナリング
背景:
- ウビキチン鎖は,タンパク質の分解と複雑な組織を含む多様な細胞プロセスを調節する.
- E2酵素 (ユビキチン結合酵素) は,ユビキチン鎖の組み立ての重要な媒介者であるが,それらの結合特異性メカニズムは不明である.
研究 の 目的:
- K11特異のE2酵素Ube2Sがユビキチン鎖形成における結合特異性を達成するメカニズムを解明する.
主な方法:
- Ube2Sとユビキチン間の非共性相互作用の役割を調査した.
- Ube2Sによるドナーと受容体のユビキチン分子の認識を分析した.
- Ube2Sとubiquitin.comの両方の貢献を通じてアクティブサイトの形成を特徴づけました.
主要な成果:
- Ube2Sは,活性部位のチオエステル結合に加えて,ドナーウビキチンをオリエンテーションするために,非共性相互作用を使用します.
- 静電相互作用は,Ube2S-ドナーユビキチン複合体による受容体ユビキチンの一時的な認識を媒介する.
- Lys11の周りの受容体ユビキチン表面の認識によって,Ube2Sとユビキチンの両方の残留物を含む触媒的に有能な活性サイトが形成されます.
結論:
- Ube2SなどのモノメリックE2酵素は,結合特異的なユビキチン鎖の形成を促進するために,基板補助触媒を使用します.
- このメカニズムは,ユビキチン鎖のトポロジーの特異性を達成するために,非共性相互作用と酵素基板協力の重要性を強調しています.
関連する概念動画
Covalently Linked Protein Regulators
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
These groups modify specific amino acids in a protein.
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 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...
The Proteasome Structure
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The proteasome is an...

