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Related Concept Videos

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...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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...
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...

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Related Experiment Video

Updated: Jun 3, 2026

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy
05:58

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

Published on: September 6, 2024

Recognizing and remodeling the nucleosome.

Sebastian Glatt1, Claudio Alfieri, Christoph W Müller

  • 1European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, Heidelberg, Germany.

Current Opinion in Structural Biology
|March 8, 2011
PubMed
Summary
This summary is machine-generated.

Structural biology reveals how nucleosome core particles (NCPs) interact with partners. This understanding extends from histone tail modifications to complex chromatin remodeling, advancing chromatin biology insights.

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Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes
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Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes

Published on: October 25, 2014

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

Related Experiment Videos

Last Updated: Jun 3, 2026

In Situ Nucleosome Assembly for Single-Molecule Correlative Force and Fluorescence Microscopy
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Published on: September 6, 2024

Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes
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Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes

Published on: October 25, 2014

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones
09:26

Reconstitution of Nucleosomes with Differentially Isotope-labeled Sister Histones

Published on: March 26, 2017

Area of Science:

  • Structural biology
  • Chromatin biology
  • Molecular recognition

Background:

  • The X-ray structure of the nucleosome core particle (NCP) is a foundational achievement in chromatin structural biology.
  • Understanding NCP interactions has evolved from recognizing histone post-translational modifications (PTMs) to comprehending higher-order chromatin structures.
  • Multi-subunit chromatin remodeling complexes play a crucial role in modulating chromatin architecture.

Purpose of the Study:

  • To review recent advancements in the structural biology of nucleosome recognition.
  • To bridge the understanding of interactions involving individual chromatin-binding domains and complex remodeling machinery.
  • To highlight the structural basis of how proteins recognize and interact with nucleosomes.

Main Methods:

  • X-ray crystallography of nucleosome core particles.
  • Structural analysis of chromatin-binding domains.
  • Biochemical and biophysical studies of chromatin remodeling complexes.
  • Integrative structural biology approaches.

Main Results:

  • Detailed structures of NCPs bound by various proteins have been elucidated.
  • Mechanisms by which chromatin-binding domains recognize histone PTMs are structurally defined.
  • Structures of multi-subunit remodeling complexes interacting with nucleosomes reveal intricate recognition strategies.
  • Insights into how higher-order chromatin structures are recognized and remodeled.

Conclusions:

  • Structural biology provides critical insights into nucleosome recognition mechanisms.
  • The transition from recognizing PTMs to higher-order structures represents a significant leap in understanding chromatin regulation.
  • Continued structural studies are essential for deciphering the complexities of chromatin dynamics and function.