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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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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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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.
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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.
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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
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With NuRD, HDACs Go "Nerdy".

Yi Eve Sun1, Liming Cheng2, Keping Hu3

  • 1Stem Cell Translational Research Center, Tongji Hospital, Tongji University School of Medicine, Shanghai 200092, China; Department of Psychiatry and Biobehavioral Sciences, IDDRC, University of California at Los Angeles, 635 Charles E. Young Drive, Los Angeles, CA 90095, USA; Kunming Biomed International and National Engineering Research Center of Biomedicine and Animal Science, Kunming 650500, China.

Developmental Cell
|July 16, 2014
PubMed
Summary
This summary is machine-generated.

Histone deacetylases (HDACs) in neurons gain specificity through the NuRD complex. This complex is critical for shutting down synaptogenesis genes in the cerebellum, enhancing presynaptic structure differentiation.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Epigenetics

Background:

  • Gene expression regulation is crucial for neuronal development.
  • Histone deacetylases (HDACs) are key epigenetic regulators.
  • The Nucleosome Remodeling and Deacetylating (NuRD) complex is involved in gene silencing.

Purpose of the Study:

  • To investigate the role of HDAC-containing NuRD complex in cerebellar development.
  • To understand how HDACs acquire specificity in neurons.
  • To elucidate the mechanisms regulating synaptogenesis-related gene expression.

Main Methods:

  • Analysis of gene expression in cerebellar neurons.
  • Investigating the function of the NuRD complex.
  • Studying the differentiation of presynaptic structures.

Main Results:

  • The NuRD complex plays a critical role in downregulating specific synaptogenesis genes in the cerebellum.
  • HDACs appear to acquire their neuronal specificity through interaction with the NuRD complex.
  • This process leads to enhanced differentiation of presynaptic structures.

Conclusions:

  • The NuRD complex is essential for precise regulation of gene expression during cerebellar development.
  • HDAC specificity in neurons is mediated by the NuRD complex.
  • Targeted gene silencing by NuRD facilitates neuronal differentiation.