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相关概念视频

The Nucleosome Core Particle01:12

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Modification02:32

Histone Modification

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 deacetylase,...
The Nucleosome01:19

The Nucleosome

Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
In a chromosome, DNA is wound twice around a protein complex called a histone octamer core, which consists of 8 histone proteins. This...

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相关实验视频

Updated: May 18, 2026

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

不对称地修改的核细胞.

Philipp Voigt1, Gary LeRoy, William J Drury

  • 1Howard Hughes Medical Institute, New York University School of Medicine, Department of Biochemistry, New York, NY 10016, USA.

Cell
|October 2, 2012
PubMed
概括
此摘要是机器生成的。

核体可以在基因素拷贝上进行对称或不对称的修改. 这种不对称性影响基因调节和染色质状态,揭示了对表观遗传机制的新见解.

更多相关视频

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

相关实验视频

Last Updated: May 18, 2026

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

科学领域:

  • 表观遗传学和分子生物学
  • 染色体生物学 染色体生物学
  • 基因规则 基因规则

背景情况:

  • 单核细胞,染色质的基本单元,由核心组织蛋白组成,它们的翻译后修饰对于染色质依赖的过程至关重要.
  • 核细胞体内的单个组素拷贝的精确的体内修饰状态在很大程度上仍未确定.

研究的目的:

  • 为了调查核细胞体内的基因组拷贝是否在体内同样被修改.
  • 探索对称与非对称的基因组修饰的功能影响.

主要方法:

  • 从胚胎干细胞,纤维细胞和癌细胞中核细胞的分析.
  • 使用检测素H3素27二/三甲基化 (H3K27me2/3) 和H4K20me1.3的技术进行检测.
  • 通过使用直接的物理证据,研究双价恒变异,包括H3K4me3,H3K36me3和H3K27me3.

主要成果:

  • 核细胞体表现出对称和不对称地修饰的H3K27me2/3和H4K20me1.1种群.
  • 在对立的H3尾部发现了具有明显修饰 (H3K4me3/H3K36me3和H3K27me3) 的双价核体的直接证据.
  • 在胚胎干细胞分化后,目标基因的双相对应性得到解决.
  • 通过对称放置的H3K4me3或H3K36me3抑制了多合体抑制复杂的2介导的H3K27甲基化,但不是通过不对称放置.

结论:

  • 不对称的组织蛋白修饰可以建立不同的功能核细胞体状态.
  • 提出了一个将双价特征纳入核体的机制.
  • 基因组基因修饰不对称性在调节基因表达和染色质功能方面发挥着作用.