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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
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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Heterochromatin02:38

Heterochromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
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Duplication of Chromatin Structure02:05

Duplication of Chromatin Structure

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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.
The basic unit of the chromatin is the nucleosome, consisting of DNA wrapped around octameric histone proteins and short stretches of linker DNA separating individual nucleosomes. The histone proteins within the nucleosome have their...
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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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Euchromatin01:01

Euchromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
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Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes
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The tumour suppressor CHD5 forms a NuRD-type chromatin remodelling complex.

Venkatadri Kolla1, Koumudi Naraparaju1, Tiangang Zhuang1

  • 1*Division of Oncology, Department of Pediatrics, The Children's Hospital of Philadelphia, University of Pennsylvania, Philadelphia 19104, PA, U.S.A.

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Chromodomain helicase DNA-binding protein 5 (CHD5) forms a nucleosome remodelling and deacetylation (NuRD) complex, similar to CHD4. This complex may have unique functions in development and tumor suppression.

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Area of Science:

  • Molecular Biology
  • Cancer Research
  • Epigenetics

Background:

  • Eukaryotic gene expression is regulated by chromatin remodeling, and its disruption is linked to cancer.
  • CHD5 is a tumor suppressor gene located in a frequently deleted region in neuroblastomas.
  • CHD5 shares homology with core subunits of the NuRD complex (CHD3 and CHD4).

Purpose of the Study:

  • To investigate whether CHD5 forms a nucleosome remodeling and deacetylation (NuRD) complex.
  • To identify proteins associated with CHD5 in nuclear extracts.
  • To understand the potential role of CHD5 in tumor suppression.

Main Methods:

  • Immunoprecipitation (IP) using CHD5 or V5/histidine-tagged CHD5 antibodies.
  • GST-FOG1 pull-down assays.
  • Mass spectrometry (MS/MS) analysis.
  • Western blotting to detect NuRD components.

Main Results:

  • CHD5 was found to associate with all canonical NuRD components, including MTA1/2, GATAD2A, HDAC1/2, RBBP4/7, and MBD2/3.
  • Mass spectrometry confirmed the presence of CHD5 and other NuRD proteins, and identified novel associated proteins.
  • Data indicate CHD5 forms a NuRD complex analogous to CHD4.

Conclusions:

  • CHD5 forms a NuRD complex with characteristics similar to those of CHD4.
  • The CHD5-NuRD complex may possess unique protein interactions conferring functional specificity.
  • These interactions could contribute to normal development and tumor suppression in neuroblastomas and other cancers.