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Related Concept Videos

Nucleosome Remodeling02:54

Nucleosome Remodeling

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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.
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Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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The Nucleosome Core Particle01:12

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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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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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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
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Histone Modification02:32

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Related Experiment Video

Updated: Nov 10, 2025

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Structures of chromatin modulators in complex with nucleosome.

Jinrong Min1, Ke Liu2

  • 1Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan, 430079, PR China; Structural Genomics Consortium, University of Toronto, Toronto, Ontario, M5G 1L7, Canada; Department of Physiology, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.

Current Opinion in Chemical Biology
|April 6, 2021
PubMed
Summary

Understanding chromatin structure is key to DNA processes. This review highlights recent 3D structural studies of chromatin modulators, like histone demethylases (LSD1/2), bound to nucleosomes, advancing insights into gene regulation.

Keywords:
ChromatinComplex structureHistoneNucleosome

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Sequential Salt Extractions for the Analysis of Bulk Chromatin Binding Properties of Chromatin Modifying Complexes
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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Epigenetics

Background:

  • Chromatin structure dynamically regulates DNA accessibility and nuclear processes.
  • Post-translational histone modifications, histone variants, and DNA unwinding are key regulatory mechanisms.
  • Understanding these modulators' structures is crucial for deciphering their function.

Purpose of the Study:

  • To review recent advancements in determining the 3D structures of chromatin modulators complexed with nucleosomes.
  • To highlight structural insights into specific modulators like LSD1/2, pioneer transcription factors, and LEDGF.

Main Methods:

  • Review of recent structural biology studies.
  • Analysis of high-resolution 3D structural data (e.g., X-ray crystallography, cryo-EM).
  • Focus on nucleosome-modulator complexes.

Main Results:

  • Recent structural studies provide detailed views of chromatin modulators interacting with nucleosomes.
  • Structures reveal mechanisms of histone modification, variant incorporation, and DNA unwinding.
  • Specific examples include histone demethylases (LSD1/2), pioneer transcription factors, and LEDGF.

Conclusions:

  • Structural studies of nucleosome-modulator complexes are essential for understanding chromatin regulation.
  • These insights facilitate comprehension of DNA-templated nuclear processes.
  • Continued structural investigation will illuminate epigenetic mechanisms and gene control.