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相关概念视频

Histone Modification02:32

Histone Modification

13.3K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
13.3K
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

4.3K
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
4.3K
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

4.0K
The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate...
4.0K
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.1K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.1K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

8.3K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
8.3K
Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

6.2K
Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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相关实验视频

Updated: Jun 29, 2025

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
07:02

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

Published on: December 16, 2021

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迪内因轻中间链表现出不同的氨酸甲基化模式.

Weiwen Bu1, Jie Di1, Junkui Zhao1

  • 1Department of Genetics and Cell Biology, Haihe Laboratory of Cell Ecosystem, State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences, Nankai University, Tianjin, China.

Journal of clinical laboratory analysis
|March 25, 2024
PubMed
概括
此摘要是机器生成的。

迪内因机动蛋白子单元LIC2通过PRMT1.1在阿尔金宁397得到甲基化. 这种翻译后修改 (PTM) 提供了关于dynein运输调节和疾病相关性的见解.

关键词:
在PRMT1中,氨酸甲基化的阿尔金因.这就是Dynein.轻型中链轻型中链链微管是微管中的一个.

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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

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In vitro Methylation Assay to Study Protein Arginine Methylation
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In vitro Methylation Assay to Study Protein Arginine Methylation

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相关实验视频

Last Updated: Jun 29, 2025

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy

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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells
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Quantitative Methods to Study Protein Arginine Methyltransferase 1-9 Activity in Cells

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In vitro Methylation Assay to Study Protein Arginine Methylation
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科学领域:

  • 细胞生物学 细胞生物学
  • 蛋白质功能的分子机制
  • 神经科学与疾病

背景情况:

  • 运动蛋白质dynein促进了沿着微管的逆行运输,通过适应蛋白与各种货物相互作用.
  • 迪内因轻中间链子单元 (LIC1和LIC2) 调解这些相互作用,形成具有独特和重叠功能的独特复合体.

研究的目的:

  • 为了研究dynein轻中间链子单元 (LIC1和LIC2) 的翻译后修改 (PTM).
  • 为了确定LIC2上的特定甲基化位点和负责这些修改的酶.
  • 了解PTM如何调节dynein功能及其对疾病的影响.

主要方法:

  • 对LIC1和LIC2C终端域 (CTD) 的生物信息分析.
  • 免疫沉和免疫阻塞,以评估LIC2甲基化状态和相关蛋白质.
  • 部位定向突变发生,以确定LIC2.2上特定的甲基化部位.

主要成果:

  • 与LIC1.1相比,LIC2表现出不同的PTM.
  • 具体来说,LIC2在阿尔金宁397.7的水平上是甲基化.
  • 蛋白质氨酸甲基转移酶1 (PRMT1) 催化LIC2在氨酸397.7的甲基化.

结论:

  • LIC子单位的独特PTM提供了用于dynein介导货物运输的多功能机制.
  • 了解LIC2 PTMs,特别是R397的甲基化,对于阐明dynein在疾病中的作用至关重要.
  • 这一发现加深了我们对通过PTMs调节dynein复合物的理解.