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Related Concept Videos

Histone Modification02:32

Histone Modification

13.0K
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...
13.0K
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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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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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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Euchromatin01:01

Euchromatin

6.8K
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
6.8K
Heterochromatin02:38

Heterochromatin

9.5K
The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at...
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Updated: May 24, 2025

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
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Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

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Connected Chromatin Amplifies Acetylation-Modulated Nucleosome Interactions.

Rina Li1, Xingcheng Lin1,2

  • 1Department of Physics, North Carolina State University, Raleigh, North Carolina 27607, United States.

Biochemistry
|March 3, 2025
PubMed
Summary
This summary is machine-generated.

Histone acetylation, specifically H4K16ac, stabilizes nucleosomes and weakens interactions between them. This leads to chromatin decompaction, promoting gene transcription by exposing nucleosomes.

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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
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Area of Science:

  • Molecular Biology
  • Biophysics
  • Chromatin Dynamics

Background:

  • Histone acetylation is a critical epigenetic mark regulating gene transcription.
  • H4K16 acetylation (H4K16ac) is a known marker for gene activation and open chromatin.
  • The impact of H4K16ac on higher-order chromatin structure remains incompletely understood.

Purpose of the Study:

  • To investigate how histone tail modifications, specifically H4K16ac, influence nucleosome stability and higher-order chromatin organization.
  • To bridge the gap between local chemical modifications and global chromatin structure.

Main Methods:

  • Utilized a residue-resolution coarse-grained chromatin model.
  • Employed enhanced sampling techniques to simulate acetylation effects.
  • Simulated nucleosome stability, internucleosome interactions, and chromatin structure.

Main Results:

  • H4K16ac stabilizes individual nucleosomes by reducing histone tail entropy during DNA unwrapping.
  • Acetylation weakens internucleosome interactions by decreasing contacts between histone tails, DNA, and acidic patches.
  • Weakened interactions, amplified by linker DNA, cause chromatin destacking and decompaction, increasing accessibility for transcription.

Conclusions:

  • Histone acetylation, particularly H4K16ac, plays a significant role in regulating chromatin structure and accessibility.
  • The geometric constraints of DNA within chromatin are crucial for mediating structural changes induced by post-translational modifications.