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Related Concept Videos

Histone Modification02:32

Histone Modification

15.8K
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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Histone Modification02:32

Histone Modification

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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...
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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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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.1K
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...
2.1K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

14.0K
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...
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Related Experiment Video

Updated: Jan 6, 2026

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

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Aggregated NETs Sequester and Detoxify Extracellular Histones.

Jasmin Knopf1, Moritz Leppkes2, Georg Schett1

  • 1Department of Medicine 3 - Rheumatology and Immunology, Universitätsklinikum Erlangen, Erlangen, Germany.

Frontiers in Immunology
|October 2, 2019
PubMed
Summary
This summary is machine-generated.

Neutrophils release Neutrophil Extracellular Traps (NETs) composed of DNA and histones. Aggregated NETs (aggNETs) remove extracellular histones, potentially mitigating their toxicity in inflammatory diseases.

Keywords:
NET formationaggNETsautoimmunityhistonesproteolysissepsis

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Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Neutrophils release Neutrophil Extracellular Traps (NETs) in response to stimuli.
  • NETs are scaffolds of DNA and histones, with extracellular histones potentially causing toxicity.
  • Aggregated NETs (aggNETs) are enzymatically active structures formed at high neutrophil densities.

Purpose of the Study:

  • To investigate the fate of extracellular histones in the context of aggNETs.
  • To understand the implications of histone removal by aggNETs for neutrophil-driven diseases and inflammation resolution.

Main Methods:

  • Observation of aggNET formation in vitro.
  • Analysis of histone removal from culture supernatants containing aggNETs.

Main Results:

  • Externally added histones are removed from culture supernatants of aggNETs.
  • aggNETs actively process and potentially sequester extracellular histones.

Conclusions:

  • aggNETs play a role in managing extracellular histones, which may have implications for disease pathogenesis.
  • Understanding histone fate during NET formation is crucial for resolving inflammation and treating related diseases.