相关实验视频
Updated: May 16, 2026

08:33
Ubiquitin Chain Analysis by Parallel Reaction Monitoring
Published on: June 17, 2020
乌比基链形状调节相互作用蛋白的识别和活性
Yu Ye1, Georg Blaser, Mathew H Horrocks
1Division of Protein and Nucleic Acids Chemistry, MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Nature
|December 4, 2012
概括
蛋白质无化涉及到以不同的形状存在的动态无链. 这些先前存在的状态被相互作用的蛋白质所识别,从而影响生物调节.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 结构生物学 结构生物学
背景情况:
- 蛋白质识别机制在单域蛋白质方面得到了很好的研究,但在动态多域系统方面却得到了较少的研究.
- 乌比基链是由各种与乌比基相互作用的蛋白质识别的关键多域系统.
- 在孤立状态和与蛋白质结合的复合体之间,乌比奎丁链形状不同,这表明灵活性或重塑.
研究的目的:
- 为了研究溶液中不同泛素链链的构造状态.
- 为了确定与ubiquitin相互作用的蛋白质是否选择先前存在的构造或诱导重塑.
- 了解形态平衡在无处不在链识别和调节中的作用.
主要方法:
- 单分子光共振能量转移 (smFRET) 用于研究二维基的构成.
- 在溶液中分析Lys63-,Lys48-和Met1结合的二维基素.
- 研究duibiquitin和ubiquitin结合域/deubiquitinases (DUBs) 之间的相互作用.
主要成果:
- 与lys63-和met1结合的duibiquitin存在于不同的"开放"和"关闭"形状.
- 乌比奎丁结合域和DUB选择这些预先存在的形状.
- 与lys48结合的diubiquitin主要采用紧的形状,而DUB可以重塑这些链.
- 破坏Lys48-diubiquitin接口会改变动态和DUB活动.
结论:
- 乌比奎链中的形态平衡在乌比奎系统中提供了一个额外的调节层.
- 不同连接的多基因的不同构造有助于基因相互作用蛋白的特异性.
- 了解这些构造动态对于破译泛素信号通路至关重要.
相关概念视频
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...
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.
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 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
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...

