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Related Concept Videos

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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The Nucleosome Core Particle02:10

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.
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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Histone Modification02:32

Histone Modification

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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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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 Nucleosome01:19

The Nucleosome

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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...
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Related Experiment Video

Updated: Mar 28, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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[Structure and function of histone chaperone FACT].

M T Bondarenko1,2, N V Maluchenko3, M E Valieva3

  • 1Fox Chase Cancer Center, Philadelphia, PA, 19111-2497 United States.

Molekuliarnaia Biologiia
|December 30, 2015
PubMed
Summary

The FACT protein complex acts as a histone chaperone, crucial for maintaining and remodeling chromatin structure during DNA processes like transcription and replication. It ensures nucleosome integrity and facilitates cell transformation and tumor cell viability.

Keywords:
FACTchromatinhistones H2A-H2Btranscription

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Dynamics

Context:

  • The FACT (Facilitates Chromatin Transcription) complex is a heterodimer protein essential for DNA-dependent cellular processes.
  • It functions as a histone chaperone, playing a critical role in chromatin maintenance and modification.

Purpose:

  • To elucidate the role of the FACT complex in nucleosome dynamics during DNA replication, transcription, and repair.
  • To understand how FACT facilitates nucleosome preservation and remodeling.

Summary:

  • FACT interacts with histone H2A-H2B dimers to facilitate DNA uncoiling from nucleosomes during transcription elongation.
  • It reduces nucleosome barrier height, aiding RNA polymerase II passage and ensuring nucleosome survival.
  • FACT also assists in the recovery of canonical nucleosome structure post-transcription.

Impact:

  • FACT is vital for maintaining chromatin structure during essential cellular processes.
  • The complex plays a significant role in human cell transformation.
  • It is implicated in sustaining the viability of tumor cells, suggesting potential therapeutic relevance.