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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...
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,...

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Related Experiment Video

Updated: May 10, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

A common structural theme in histone chaperones mimics interhistone contacts.

Simon J Elsässer1

  • 1MRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK. selsaess@mrc-lmb.cam.ac.uk

Trends in Biochemical Sciences
|June 25, 2013
PubMed
Summary
This summary is machine-generated.

Histones, essential for DNA packaging, have evolved specialized surfaces for regulation. Histone chaperones like DAXX, HJURP, and Scm3 reuse structural themes to interact with these conserved proteins, enabling chromatin function modulation.

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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Related Experiment Videos

Last Updated: May 10, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

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

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:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Histones are highly conserved eukaryotic proteins crucial for nucleosome structure.
  • The constrained surfaces of histones present evolutionary challenges for novel function development.
  • Specialized histone chaperones modulate basic chromatin function by interacting with histones.

Purpose of the Study:

  • To investigate the structural basis of histone-chaperone interactions.
  • To understand how confined histone surfaces diversify to allow functional modulation.
  • To exemplify evolutionary solutions in histone recognition by chaperones.

Main Methods:

  • Analysis of recent structures of three histone-chaperone complexes: DAXX, HJURP, and Scm3.
  • Comparative structural biology to identify common themes in histone recognition.
  • Examination of evolutionary constraints and diversification of histone surfaces.

Main Results:

  • Structures reveal DAXX, HJURP, and Scm3 utilize conserved structural motifs for histone binding.
  • These chaperones demonstrate a parsimonious evolutionary strategy for recognizing restricted histone surfaces.
  • The findings highlight the reutilization of existing structural themes in histone-chaperone complex evolution.

Conclusions:

  • Histone chaperones employ a limited set of structural solutions to interact with conserved histone surfaces.
  • This reutilization of structural themes allows for the evolution of specialized chromatin regulatory functions.
  • The study provides insights into the evolutionary adaptability of chromatin-associated proteins.