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相关概念视频

Histone Modification02:32

Histone Modification

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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...
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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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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...
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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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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...
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Nucleosome Remodeling02:54

Nucleosome Remodeling

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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...
9.1K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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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...
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Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

1.7K
Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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相关实验视频

Updated: Jul 4, 2025

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

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人类SRCAP复合体对组织激素交换的结构洞察力

Jiali Yu1,2, Fengrui Sui1, Feng Gu1

  • 1Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, New Cornerstone Science Laboratory, State Key Laboratory of Genetic Engineering and Shanghai Key Laboratory of Medical Epigenetics, Shanghai Medical College of Fudan University, Shanghai, China.

Cell discovery
|February 8, 2024
PubMed
概括
此摘要是机器生成的。

该SRCAP复合体 (SRCAP-C) 在促进器处用H2A.Z取代组合素H2A,以调节转录. 结构研究揭示了SRCAP-C如何破坏稳定并去除H2A-H2B二元体,从而促进H2A.Z的结合.

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科学领域:

  • 染色体生物学 染色体生物学
  • 转录调节的分子机制
  • 结构生物学是结构生物学.

背景情况:

  • 基因组突变H2A.Z对于基因转录调节至关重要.
  • 该SRCAP复合体 (SRCAP-C) 促进了正规H2A-H2B二元体与H2A.Z-H2B二元体的交换.
  • 了解这种交换的结构基础是破译转录控制的关键.

研究的目的:

  • 确定人体SRCAP-C与含有H2A的核细胞结合的近原子分辨率结构.
  • 阐明SRCAP-C调解H2A-H2A.Z交换的分子机制.

主要方法:

  • 接近原子分辨率的冷电子显微镜 (cryo-EM) 人类SRCAP-C结合于核体.
  • 生物化学试验用于研究ATPase活性和核酶结合模式.
  • 结构指导的染色体免疫沉测序 (ChIP-seq) 来评估基因组H2A.Z占用率.

主要成果:

  • 该SRCAP子单元包括一个与乙烯相关蛋白 (ARP) 模块和一个ATPase电机模块.
  • 该ARP模块围绕着核细胞DNA,可能抑制DNA转位.
  • 运动模块在不同核酸结合状态中的不同结合模式显示出一种由ATPase驱动的机制,该机制通过ZNHIT1子单元破坏稳定并提取H2A-H2B.
  • 结构引导的CHIP-seq证实了ZNHIT1在维持H2A.Z基因组占用中的作用.

结论:

  • 这项研究为通过SRCAP-C.介导的H2A-H2A.Z交换机制提供了前所未有的结构洞察力.
  • 这些发现揭示了SRCAP-C如何利用ATPase活动来重塑核细胞和调节转录.
  • ZNHIT1被确定为基因组中H2A.Z维护的关键组成部分.