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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
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Histone Modification02:32

Histone Modification

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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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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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Abnormal Proliferation02:23

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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
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The Retinoblastoma Gene01:20

The Retinoblastoma Gene

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Tumor suppressor genes are normal genes that can slow down cell division, repair DNA mistakes, or program the cells for apoptosis in case of irreparable damage. Hence, they play an essential role in preventing the proliferation of damaged cells.
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Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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The Oncoprotein BRD4-NUT Generates Aberrant Histone Modification Patterns.

Barry M Zee1,2, Amy B Dibona3, Artyom A Alekseyenko1,2

  • 1Department of Genetics, Harvard Medical School, Boston, Massachusetts, United States of America.

Plos One
|October 5, 2016
PubMed
Summary
This summary is machine-generated.

NUT-midline carcinoma (NMC) involves BRD4-NUT (B4N) fusion proteins altering chromatin. This study found B4N complexes modify histone posttranslational modifications, potentially driving aberrant transcription in NMC.

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Examination of Proteins Bound to Nascent DNA in Mammalian Cells Using BrdU-ChIP-Slot-Western Technique
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cancer Biology

Background:

  • Defects in chromatin proteins are linked to various diseases.
  • NUT-midline carcinoma (NMC) is a chromatin-centric cancer characterized by NUT-BRD4 fusions.
  • BRD4-NUT (B4N) fusion proteins in NMC are known to occupy large genomic regions and enhance transcription.

Purpose of the Study:

  • To investigate the mechanism by which BRD4-NUT (B4N) modulates chromatin.
  • To identify the specific histone posttranslational modifications (PTMs) associated with B4N.

Main Methods:

  • Ectopic expression of B4N in 293-TREx cells.
  • Affinity purification of B4N complexes.
  • Proteomic analysis to quantify associated histone PTMs.

Main Results:

  • Significant enrichment of H3 K18 acetylation was observed.
  • Combinatorial patterns, including H3 K27 acetylation with H3 K36 methylation, were identified.
  • B4N complexes are associated with distinct PTM profiles.

Conclusions:

  • B4N complexes may override the existing histone code with novel PTM patterns.
  • These aberrant PTMs likely reflect and drive aberrant transcription in NMC.
  • Epigenetic modulation of the nucleosome environment by B4N contributes to the NMC state.