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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.
Nucleosome remodeling complex
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The Nucleosome Core Particle01:12

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.
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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.
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Duplication of Chromatin Structure02:05

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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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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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The Nucleosome02:33

The Nucleosome

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DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
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Related Experiment Video

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Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
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Structure and function insights into the NuRD chromatin remodeling complex.

Morgan P Torchy1, Ali Hamiche, Bruno P Klaholz

  • 1Department of Integrated Structural Biology, Centre for Integrative Biology (CBI), Institute of Genetics and of Molecular and Cellular Biology (IGBMC), 1 rue Laurent Fries, Illkirch, France.

Cellular and Molecular Life Sciences : CMLS
|March 23, 2015
PubMed
Summary
This summary is machine-generated.

The nucleosome remodeling and histone deacetylation (NuRD) complex regulates transcription via chromatin remodeling. This review covers NuRD subunit structures and functions, highlighting its role in diseases like cancer.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Structural Biology

Background:

  • Transcription regulation is crucial for cellular function.
  • Chromatin remodeling complexes, like NuRD, play key roles in modulating DNA accessibility.
  • The NuRD complex is a large, multi-subunit assembly involved in gene silencing.

Purpose of the Study:

  • To review the structural and functional data of NuRD complex subunits.
  • To discuss the biomedical relevance of NuRD in diseases, particularly cancer.
  • To highlight the challenges and future directions in studying NuRD structure-function relationships.

Main Methods:

  • Literature review of existing crystal and NMR structures.
  • Analysis of functional data for individual NuRD subunits.
  • Integration of structural and functional information to understand complex assembly.

Main Results:

  • Detailed overview of known structures for key NuRD subunits (e.g., HDAC1/2, CHD3/4, RbAp46/48, MBD2/3, GATAD2a/b, MTA1/2/3).
  • Functional insights into the roles of these subunits in chromatin remodeling and gene regulation.
  • Evidence linking NuRD subunit dysfunction to various diseases, including cancer.

Conclusions:

  • The NuRD complex's intricate structure presents significant challenges for understanding its nucleosome interaction.
  • An integrated biology approach is essential for elucidating NuRD's structure-function relationships.
  • Further research into NuRD is critical for developing novel therapeutic strategies for associated diseases.