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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

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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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Inheritance of Chromatin Structures03:17

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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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Epigenetic Regulation01:37

Epigenetic Regulation

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Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...
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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Folate deficiency affects histone methylation.

Benjamin A Garcia1, Zigmund Luka2, Lioudmila V Loukachevitch3

  • 1Epigenetics Program, Departments of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, 3400 Civic Center Blvd, Philadelphia, PA 19104, USA.

Medical Hypotheses
|February 17, 2016
PubMed
Summary
This summary is machine-generated.

Tetrahydrofolate (THF) protects histone demethylase LSD1 from toxic formaldehyde by forming 5,10-methylene-THF. Folate deficiency increases methylated histone levels, suggesting THF’s crucial role beyond one-carbon metabolism in epigenetic regulation and disease.

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Immunostaining for DNA Modifications: Computational Analysis of Confocal Images
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Immunostaining for DNA Modifications: Computational Analysis of Confocal Images

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Area of Science:

  • Biochemistry
  • Epigenetics
  • Molecular Biology

Background:

  • Formaldehyde is a toxic metabolic byproduct that can damage proteins.
  • Enzymes generating formaldehyde require protection mechanisms.
  • Histone lysine demethylase 1 (LSD1) produces formaldehyde during demethylation of histone H3 lysine 4.

Purpose of the Study:

  • To investigate if tetrahydrofolate (THF) scavenges formaldehyde produced by LSD1.
  • To test the hypothesis that bound THF protects FAD-dependent histone demethylases from formaldehyde.
  • To explore the link between folate deficiency, LSD1 activity, and histone methylation levels.

Main Methods:

  • Enzyme assays comparing DMGDH/SDH with LSD1.
  • Analysis of formaldehyde scavenging by THF.
  • Dietary folate deficiency model in rodents.
  • Measurement of histone H3 lysine 4 methylation levels.

Main Results:

  • Pilot data show dietary folate deficiency correlates with increased histone H3 lysine 4 methylation.
  • This suggests reduced LSD1 activity due to insufficient THF for formaldehyde scavenging.
  • THF forms 5,10-methylene-THF, effectively removing formaldehyde.

Conclusions:

  • Bound THF likely protects FAD-dependent histone demethylases like LSD1 from self-generated formaldehyde.
  • Folate deficiency may impair LSD1 function, impacting gene expression.
  • Folate's role in epigenetic regulation and associated diseases warrants further investigation.