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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
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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

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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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The Nucleosome02:33

The Nucleosome

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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...
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Related Experiment Video

Updated: Mar 31, 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

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H1-nucleosome interactions and their functional implications.

Jan Bednar1, Ali Hamiche2, Stefan Dimitrov3

  • 1Université de Grenoble Alpes/CNRS, Laboratoire Interdisciplinaire de Physique, UMR 5588, 140 rue de la Physique, B.P. 87, St. Martin d'Heres, F-38402, France.

Biochimica Et Biophysica Acta
|October 20, 2015
PubMed
Summary
This summary is machine-generated.

Linker histones are crucial for chromatin structure and gene regulation. Their binding to nucleosomes and chromatin fibers, along with post-translational modifications, influences function, though mechanisms remain under investigation.

Keywords:
Gene expression regulationLinker histoneLinker histone bindingLinker histone subtypes

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Area of Science:

  • Molecular Biology
  • Chromatin Biology
  • Epigenetics

Background:

  • Linker histones are essential proteins for the assembly and maintenance of the condensed chromatin fiber.
  • Their structured globular domain interacts with DNA and the nucleosome, while the COOH-terminus closes the linker DNA.
  • The precise binding mode within the chromatin fiber and the functional impact of their high in vivo mobility are not fully understood.

Purpose of the Study:

  • To summarize and analyze existing data on linker histone binding to nucleosomes and chromatin fibers.
  • To discuss the functional consequences of linker histone binding and post-translational modifications.
  • To explore the implications of linker histone mobility in vivo versus in vitro.

Main Methods:

  • Characterization of linker histone binding to nucleosomes using various solution-based methods.
  • Analysis of post-translational modifications and their effects on histone function.
  • Review and synthesis of current literature on linker histone behavior and function.

Main Results:

  • Linker histones possess a structured globular domain and flexible termini involved in nucleosome binding.
  • The COOH-terminus of linker histones plays a role in closing linker DNA and forming a stem structure.
  • Linker histones are essential for chromatin condensation, gene regulation, and are subject to functional post-translational modifications.

Conclusions:

  • Linker histones are vital for chromatin organization and gene expression, with their functions modulated by post-translational modifications.
  • Further research is needed to elucidate the detailed mechanisms of linker histone function and the implications of their dynamic behavior in chromatin.
  • Understanding linker histone binding and function is key to comprehending chromatin-related processes and gene regulation.