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Related Concept Videos

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.
Acetylation
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Spreading of Chromatin Modifications02:25

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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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Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

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Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Chromatin Position Affects Gene Expression02:35

Chromatin Position Affects Gene Expression

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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. 
Topologically Associated Domains (TADs)
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Histone Acetylation Differentially Modulates CTCF-CTCF Loops and Intra-TAD Interactions.

Rebecca G Smith1,2,3, Yu Fu4, Kathleen L Schiela1,2,3

  • 1Cancer Epigenetics Institute, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.

Biorxiv : the Preprint Server for Biology
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Histone hyperacetylation disrupts cohesin (protein complex) within TADs but spares CTCF-anchored loops. This reveals two distinct cohesin states: a dynamic extruding form and a stable, topologically bound form maintaining genome structure.

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Area of Science:

  • Genomics
  • Molecular Biology
  • Epigenetics

Background:

  • The cohesin complex organizes the genome by forming loops and topologically associating domains (TADs).
  • The impact of chromatin state on cohesin's genome structuring functions is not fully understood.

Purpose of the Study:

  • To investigate how histone acetylation, induced by trichostatin A (TSA), affects cohesin's interaction with chromatin.
  • To differentiate between cohesin populations involved in TAD formation and CTCF-anchored loops.

Main Methods:

  • Induction of histone hyperacetylation using trichostatin A (TSA).
  • Analysis of cohesin occupancy and chromatin interactions using a semi-in vitro system with TEV-cleavable RAD21.
  • Distinguishing between TSA-sensitive and TSA-resistant cohesin populations.

Main Results:

  • Histone hyperacetylation disrupts short-range interactions within TADs but preserves CTCF-anchored loops.
  • Two distinct cohesin populations were identified: TSA-sensitive (extruding) and TSA-resistant (topologically bound).
  • Proteolytic cleavage of cohesin at CTCF sites rendered it TSA-sensitive, confirming the role of topological engagement.

Conclusions:

  • Cohesin exists in distinct biochemical states, influencing its role in genome organization.
  • A TSA-sensitive, extruding cohesin form allows dynamic chromatin loop changes.
  • A TSA-resistant, topologically bound cohesin form ensures the stability of CTCF-anchored loops against chromatin state alterations.