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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...
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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.
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The Nucleosome Core Particle02:10

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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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Eukaryotic Transcription Activators

Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate domains ‒ a domain that binds to DNA and a domain for activating transcription; however, in some cases, a single domain is responsible for both binding and activation of transcription, as seen in the glucocorticoid receptor and MyoD.
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RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...

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Related Experiment Video

Updated: Jul 4, 2026

A Method to Study de novo Formation of Chromatin Domains
07:34

A Method to Study de novo Formation of Chromatin Domains

Published on: August 23, 2019

Nucleosomes as active platforms for pioneer factor action.

Di Niu1, Wulan Deng1

  • 1State Key Laboratory for Gene Function and Modulation Research, Biomedical Pioneering Innovation Center (BIOPIC), Peking-Tsinghua Center for Life Sciences (CLS), Beijing Advanced Innovation Center of Genomics, School of Life Sciences, Peking University, Beijing, 100871 China.

Molecular Cell
|July 2, 2026
PubMed
Summary
This summary is machine-generated.

Pioneer transcription factor Ascl1-E12a uses nucleosomes as platforms to open chromatin. This mechanism facilitates neural reprogramming by controlling DNA accessibility.

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Area of Science:

  • Molecular biology
  • Epigenetics
  • Developmental neuroscience

Background:

  • Pioneer transcription factors initiate cell fate changes.
  • Chromatin accessibility is crucial for gene regulation.
  • Neural reprogramming requires precise control of gene expression.

Purpose of the Study:

  • To elucidate the mechanism by which the pioneer transcription factor Ascl1-E12a interacts with nucleosomes.
  • To understand how these interactions lead to chromatin opening.
  • To investigate the role of this process in neural reprogramming.

Main Methods:

  • Biochemical assays to study protein-DNA-nucleosome interactions.
  • Structural biology techniques to visualize factor-nucleosome complexes.
  • Cellular assays to assess chromatin accessibility and reprogramming efficiency.

Main Results:

  • Ascl1-E12a utilizes nucleosomes as active platforms for association.
  • Distinct histone-contacting modes enable stepwise DNA unwrapping.
  • Nucleosome repositioning by Ascl1-E12a facilitates chromatin opening.

Conclusions:

  • Ascl1-E12a employs a novel mechanism involving nucleosome exploitation for chromatin modulation.
  • This process is critical for initiating neural reprogramming.
  • Understanding this interaction provides insights into epigenetic regulation during cell fate determination.