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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.
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The writer...
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Phase II Reactions: Methylation Reactions01:17

Phase II Reactions: Methylation Reactions

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Methylation is a phase II biotransformation process involving the attachment of a methyl group to a substrate. Enzymes known as methyltransferases orchestrate this reaction.
The mechanism of methylation unfolds in two stages. The first stage sees a methyltransferase enzyme facilitating the transfer of a methyl group from S-adenosylmethionine (SAM) to the substrate, forming S-adenosylhomocysteine (SAH). The second stage involves further metabolism of SAH into homocysteine, which can be recycled...
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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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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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8 Demethylation pathways for histone methyllysine residues.

Federico Forneris1, Claudia Binda1, MariaAntonietta Vanoni2

  • 1Dipartimento di Genetica e Microbiologia Università di Pavia Via Ferrata 1 Pavia 27100, Italy.

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Summary

Histone lysine methylation is reversible, as shown by the discovery of lysine specific histone demethylase 1 (LSD1). This enzyme

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Area of Science:

  • Epigenetics
  • Molecular Biology
  • Biochemistry

Background:

  • Histone lysine methylation is a key epigenetic modification regulating gene expression and chromatin structure.
  • The discovery of lysine specific histone demethylase 1 (LSD1) challenges the notion of permanent epigenetic marks.
  • LSD1 functions within large corepressor complexes involved in stable gene silencing.

Purpose of the Study:

  • To characterize the biochemical properties of the first identified histone demethylase, LSD1.
  • To investigate the enzymatic activity and substrate specificity of LSD1.
  • To explore the implications of LSD1's function in epigenetic regulation.

Main Methods:

  • Biochemical assays were developed to study the demethylation reaction catalyzed by LSD1.
  • Analysis of LSD1's modular protein structure, including its SWIRM and FAD-dependent oxidase domains.
  • Investigating LSD1's association with corepressor proteins like CoREST and histone deacetylases.

Main Results:

  • LSD1 specifically catalyzes the oxidative demethylation of Lysine 4 on histone H3.
  • LSD1 exhibits a modular structure with domains mediating protein interactions and enzymatic activity.
  • The study established assays to analyze LSD1's biochemical properties.

Conclusions:

  • Histone methylation is a dynamic and reversible epigenetic mark.
  • LSD1 plays a crucial role in transcriptional regulation by removing methyl groups from histone H3.
  • The specific substrate recognition of LSD1 suggests the existence of other histone demethylases with diverse regulatory mechanisms.