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Related Concept Videos

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...
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...
The Nucleosome02:33

The Nucleosome

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.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
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,...

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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

Single-molecule tools elucidate H2A.Z nucleosome composition.

Jiji Chen1, Andrew Miller, Ann L Kirchmaier

  • 1Department of Agricultural and Biological Engineering, Purdue University Center for Cancer Research, 225 South University Street, West Lafayette, IN 47907, USA.

Journal of Cell Science
|March 7, 2012
PubMed
Summary
This summary is machine-generated.

This study reveals how epigenetic marks combine on single nucleosomes using advanced single-molecule techniques. It identifies specific histone modifications associated with H2A.Z nucleosomes, crucial for gene regulation.

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Last Updated: May 24, 2026

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Published on: March 9, 2022

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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

Area of Science:

  • Epigenetics
  • Molecular Biology
  • Chromatin Biology

Background:

  • Distinct epigenetic marks correlate with specific chromatin states.
  • The integration of these marks within single nucleosomes is poorly understood.
  • Histone variant H2A.Z plays a role in chromatin regulation.

Purpose of the Study:

  • To elucidate the composition of single nucleosomes containing histone variant H2A.Z.
  • To investigate the combinatorial patterns of epigenetic modifications on these nucleosomes.
  • To establish methods for quantifying epigenetic modifications at the nucleosome level.

Main Methods:

  • Utilized single-molecule tools: fluorescence correlation spectroscopy (FCS), pulse interleave excitation-based Förster resonance energy transfer (PIE-FRET), and fluorescence lifetime imaging-based FRET (FLIM-FRET).
  • Applied these methods both in vitro and in vivo.
  • Studied nucleosomes containing the histone variant H2A.Z (Htz1p in yeast).

Main Results:

  • Demonstrated that yeast nucleosomes containing Htz1p are primarily composed of H4 K12ac and H3 K4me3.
  • Showed the absence of H3 K36me3 in Htz1p-containing nucleosomes.
  • Confirmed conservation of these epigenetic modification patterns in mammalian cells.

Conclusions:

  • Quantification of epigenetic modifications in nucleosomes offers a new dimension to epigenetics research.
  • Understanding these patterns is key to comprehending chromatin-binding protein targeting.
  • Elucidating nucleosome composition aids in understanding chromatin structure and gene regulation.