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Related Concept Videos

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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The Nucleosome Core Particle01:12

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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.
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The Nucleosome Core Particle02:10

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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.
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The Nucleosome01:19

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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.
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The Nucleosome02:33

The Nucleosome

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DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to 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.
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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
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Histone succinylation and its function on the nucleosome.

Jiayi Liu1,2, Yu Shangguan1,3, Donge Tang1,2,3

  • 1Clinical Medical Research Center, Guangdong Provincial Engineering Research Center of Autoimmune Disease Precision Medicine, Shenzhen Engineering Research Center of Autoimmune Disease, The First Affiliated Hospital(Shenzhen People's Hospital), Southern University of Science and Technology, Shenzhen, China.

Journal of Cellular and Molecular Medicine
|June 23, 2021
PubMed
Summary
This summary is machine-generated.

Histone lysine succinylation (Ksucc) is a newly identified post-translational modification impacting gene expression and chromatin structure. This review explores Ksucc sites, mechanisms, and its role in diseases, highlighting potential therapeutic targets.

Keywords:
desuccinylationhistonenucleosomesuccinylation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Histone post-translational modifications (PTMs) regulate crucial biological processes.
  • Lysine succinylation (Ksucc) is an emerging histone PTM identified via mass spectrometry.
  • Ksucc accumulates at transcriptional start sites and correlates with gene expression.

Purpose of the Study:

  • To review histone lysine succinylation (Ksucc) sites and characteristics.
  • To elucidate the mechanisms of Ksucc in nucleosomal structure and chromatin dynamics.
  • To discuss the role of Ksucc in various diseases and its therapeutic potential.

Main Methods:

  • Literature review of studies on histone lysine succinylation.
  • Analysis of mass spectrometry data identifying Ksucc sites.
  • Examination of existing research on Ksucc's functional and pathological roles.

Main Results:

  • Identification and characterization of lysine succinylation sites on histones.
  • Description of Ksucc's influence on histone chemical properties and nucleosome structure.
  • Evidence linking Ksucc to gene expression regulation and disease pathogenesis.

Conclusions:

  • Histone lysine succinylation is a significant epigenetic regulator.
  • Ksucc plays roles in chromatin dynamics, gene expression, and disease.
  • Further research into Ksucc as a therapeutic target is warranted.