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相关概念视频

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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....
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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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...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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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...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Anaphase Promoting Complex00:50

Anaphase Promoting Complex

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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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相关实验视频

Updated: Jul 8, 2025

In Vitro Analysis of E3 Ubiquitin Ligase Function
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多站点化决定了选择性的E2-E3配对,正如Ubc8/UBE2H-GID/CTLH组件所揭示的那样.

Jakub Chrustowicz1, Dawafuti Sherpa1, Jerry Li2

  • 1Department of Molecular Machines and Signaling, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.

Molecular cell
|December 19, 2023
PubMed
概括

酸化指导了E3-E2酶在无处不在中的合作伙伴关系. 这项研究揭示了Ubc8/UBE2H E2酶的多站点酸化如何将它们结到GID/CTLH E3酶上,确保了特定的无处不在.

关键词:
在CK2中,CK2是CK2.复杂的CTLH是一个复杂的CTLH.E2 泛素结合酶的结合酶.E3 无处不在的合酶GID复合体是一个复杂的GID.这就是UBE2H.在UBC8中,UBC8是UBC8.低温电磁波冷却器 (Cryo-EM) 是一个非常好的方法.酸化的方法是:光化.在任何地方都是无处不在的.

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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:

  • 泛基化是一种由E3和E2酶调节的关键的翻译后修饰.
  • 控制许多E3-E2酶相互作用的特定机制,特别是RING家族GID/CTLH E3泛素酶及其同类E2酶Ubc8/UBE2H,尚未完全理解.
  • 这种E3-E2复合体调节重要的细胞过程,包括酵母代谢信号和人类发育.

研究的目的:

  • 阐明GID/CTLH E3泛素酶与Ubc8/UBE2H E2酶之间特定相互作用的分子原理.
  • 调查E2酶酸化在中介这种E3-E2伙伴关系中的作用.
  • 了解这种特定的相互作用如何有助于调节无处不在.

主要方法:

  • 使用冷电子显微镜 (cryo-EM) 确定了E3-E2复合物的结构基础.
  • 生物化学测试被用来描述酶活性和相互作用接口.
  • 细胞生物学技术被用来研究细胞环境中的功能后果.

主要成果:

  • 这项研究揭示了GID/CTLH-Ubc8/UBE2H复合体的一种非常规的催化组装机制.
  • 由CK2准的Ubc8/UBE2H的多位化,特别将E2 C终端定在E3结合酶上的基本补丁上,与之前观察到的多电静态相互作用不同.
  • 这些依赖的相互作用发生在与催化场所相距的距离上,并且在进化上相互关联,使催化中心变硬,并促进基质参与.

结论:

  • 酸化依赖的多价值性对于在无处不在中建立特定的E3-E2伙伴关系至关重要.
  • 这种机制对抗脱酸化,并使催化机械变硬.
  • 这些发现提供了关于如何实现E3-E2特异性的详细分子理解,影响细胞信号传递和发育.