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Related Concept Videos

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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.
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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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Chromatin is the massive complex of DNA and proteins packaged inside the nucleus. The complexity of chromatin folding and how it is packaged inside the nucleus greatly influences  access to genetic information. Generally, the nucleus' periphery is considered transcriptionally repressive, while the cell's interior is considered a transcriptionally active area. 
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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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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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Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
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A Method to Study de novo Formation of Chromatin Domains
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Structural basis for PRC2 engagement with chromatin.

Eleanor Glancy1, Claudio Ciferri2, Adrian P Bracken1

  • 1Smurfit Institute of Genetics, Trinity College Dublin, Dublin 2, Ireland.

Current Opinion in Structural Biology
|November 24, 2020
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Summary
This summary is machine-generated.

The Polycomb Repressive Complex 2 (PRC2) is crucial for cellular identity and development. New studies reveal how its core and accessory proteins coordinate histone methylation (H3K27me1/2/3) across the genome.

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Area of Science:

  • Epigenetics and chromatin biology
  • Molecular and developmental biology

Background:

  • The Polycomb Repressive Complex 2 (PRC2) is a key epigenetic regulator essential for maintaining cellular identity during development.
  • PRC2 catalyzes histone H3 lysine 27 methylation (H3K27me1/2/3), a mark associated with gene silencing.
  • Dysregulation of PRC2 activity is implicated in human cancers and developmental disorders like Weaver Syndrome.

Purpose of the Study:

  • To review recent biochemical and structural studies on PRC2.
  • To elucidate the coordination between core and accessory PRC2 subunits.
  • To understand the mechanisms of genome-wide H3K27 methylation deposition.

Main Methods:

  • Biochemical analyses of PRC2 complex assembly and function.
  • Structural studies of PRC2 core and subassemblies (PRC2.1, PRC2.2).
  • Review of existing literature on PRC2 regulation and function.

Main Results:

  • The trimeric core (SUZ12, EED, EZH1/2) with RBBP4/7 possesses catalytic methyltransferase activity.
  • Accessory proteins organize into distinct PRC2.1 and PRC2.2 subassemblies.
  • These studies provide insights into how PRC2 subunits cooperate for precise H3K27 methylation.

Conclusions:

  • Understanding PRC2 subunit coordination is vital for comprehending its role in development and disease.
  • New structural and biochemical data illuminate the mechanisms of H3K27 methylation.
  • Further research into PRC2 regulation may offer therapeutic targets for cancers and developmental disorders.