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Related Concept Videos

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...
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...
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,...
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,...
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...

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Related Experiment Video

Updated: Jun 25, 2026

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

Structural Basis of Nucleosome Recognition and Modulation.

Rajivgandhi Sundaram1,2, Dileep Vasudevan1

  • 1Laboratory of Macromolecular Crystallography, Institute of Life Sciences, Bhubaneswar, 751023, India.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|June 23, 2020
PubMed
Summary

This review details how proteins recognize nucleosomes, the basic units of DNA packaging. Understanding these interactions is key to regulating gene expression and cellular processes.

Keywords:
acidic patchchromatin factorschromatin remodelerslinker histonesnucleosomepost-translational modificationsviral proteins

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Last Updated: Jun 25, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

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In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Structural Biology

Background:

  • Chromatin structure and dynamics are crucial for fundamental cellular processes like DNA replication, transcription, repair, and gene expression.
  • Various protein factors, including DNA and RNA polymerases, chromatin remodelers, and transcription factors, interact with nucleosomes.
  • Recent research has elucidated the molecular mechanisms by which proteins recognize nucleosomes.

Purpose of the Study:

  • To provide critical insights into the fundamental mechanisms of nucleosome recognition by diverse protein factors.
  • To highlight the significance of distinct surface epitopes on the nucleosome in mediating these interactions.

Main Methods:

  • This is a review article, synthesizing existing research on nucleosome recognition.
  • Focuses on analyzing the molecular details and structural features involved in protein-nucleosome interactions.

Main Results:

  • Protein factors recognize nucleosomes through specific DNA sequences and/or structural features.
  • Key determinants of specificity include the acidic patch, arginine anchor, histone modifications, core DNA, DNA lesions, and linker DNA.

Conclusions:

  • Specific surface features and molecular determinants govern the recognition of nucleosomes by various protein factors.
  • A comprehensive understanding of these recognition mechanisms is essential for deciphering gene regulation and cellular functions.