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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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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.
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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.
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The process of chromosome duplication during cell division requires genome-wide disruption and re-assembly of chromatin. The chromatin structure must be accurately inherited, reassembled, and maintained in the daughter cells to ensure lineage propagation.
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Histone Modification02:32

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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.
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Related Experiment Video

Updated: Dec 10, 2025

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
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Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

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Chromatin remodelling comes into focus.

Ramasubramian Sundaramoorthy1, Tom Owen-Hughes1

  • 1Centre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, Dundee, DD1 5EH, UK.

F1000Research
|September 1, 2020
PubMed
Summary

ATP-dependent chromatin remodelling enzymes use ATPase domains to interact with DNA and histones. New structures reveal how accessory subunits assemble into complexes, explaining how these motors perform distinct functions.

Keywords:
BAF.CHD1INO80SMARCASWI/SNF complexSWR1chromatin remodellingnucleosome structure

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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

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • ATP-dependent chromatin remodelling enzymes are crucial for DNA accessibility.
  • The structural details of these molecular machines were previously limited.
  • Understanding their structure is key to deciphering their function.

Purpose of the Study:

  • To elucidate the structural organization of ATP-dependent chromatin remodelling enzymes.
  • To understand how ATPase domains and accessory subunits interact within these complexes.
  • To provide a framework for understanding the functional diversity of these enzymes.

Main Methods:

  • Recent structural biology techniques (e.g., cryo-EM, X-ray crystallography) were employed.
  • Analysis of multi-subunit complexes was performed.
  • Detailed examination of ATPase domain interactions with DNA and histones was conducted.

Main Results:

  • The interaction with chromatin is primarily mediated by ATPase domains binding to specific DNA locations on nucleosomes.
  • Histone contacts are limited but critical for modulating enzyme activity.
  • Accessory domains and subunits flank the ATPase domains, forming intricate multi-subunit complexes.
  • New structural data reveals the arrangement of these subunits.

Conclusions:

  • The structure of ATP-dependent chromatin remodelling enzymes is characterized by a central ATPase motor domain.
  • Accessory subunits are essential for complex assembly and functional regulation.
  • The revealed structures provide a mechanistic basis for how a conserved motor drives diverse chromatin remodelling functions.