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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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The Nucleosome Core Particle01:12

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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The Nucleosome Core Particle02:10

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Nucleosome Remodeling02:54

Nucleosome Remodeling

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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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Investigating Histone Acetylation Stoichiometry and Turnover Rate.

J Fan1, J Baeza1, J M Denu2

  • 1School of Medicine and Public Health, Wisconsin Institute for Discovery, University of Wisconsin, Madison, WI, United States.

Methods in Enzymology
|July 18, 2016
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Summary
This summary is machine-generated.

This study introduces novel isotopic labeling and mass spectrometry methods to precisely measure histone acetylation dynamics and stoichiometry. These techniques offer a comprehensive way to study epigenetic regulation under various conditions.

Keywords:
AcetylationEpigeneticsHistoneKineticsMass spectrometryMetabolic labelingStoichiometry

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Area of Science:

  • Epigenetics and Molecular Biology
  • Biochemistry and Mass Spectrometry

Background:

  • Histone acetylation is a crucial epigenetic modification regulating DNA-templated processes like transcription.
  • This dynamic modification is controlled by histone acetyltransferases and deacetylases.

Purpose of the Study:

  • To present robust methods for comprehensively investigating histone acetylation dynamics using isotopic labeling and mass spectrometry (MS).
  • To enable both global and site-specific evaluation of dynamic histone acetylation regulation.

Main Methods:

  • Utilized (13)C-labeled acetyl-CoA precursors for metabolic labeling to determine histone acetylation turnover rates via MS.
  • Employed chemical acetylation with isotopic acetic anhydride, followed by trypsin digestion and LC-MS, for site-specific acetylation stoichiometry.
  • Combined metabolic labeling with stoichiometric analysis for a dual assessment of acetylation level and dynamics.

Main Results:

  • Developed and validated methods for comprehensive analysis of histone acetylation.
  • Enabled determination of acetylation turnover rates and site-specific stoichiometry.
  • Facilitated the evaluation of histone acetylation dynamics across genetic, dietary, and environmental perturbations.

Conclusions:

  • The presented isotopic labeling and MS-based methods provide a powerful toolkit for studying histone acetylation.
  • These techniques allow for a detailed understanding of how epigenetic modifications are dynamically regulated in response to various factors.