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Related Concept Videos

Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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 is an enzyme that can...
Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

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 DNA...
Heterochromatin02:38

Heterochromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...

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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

Variable histone modifications at the A(vy) metastable epiallele.

Dana C Dolinoy1, Caren Weinhouse, Tamara R Jones

  • 1Department of Environmental Health Sciences, University of Michigan, Ann Arbor, Michigan, USA. ddolinoy@umich.edu

Epigenetics
|July 31, 2010
PubMed
Summary

Environmental factors influence health via epigenetics. This study reveals histone modifications, alongside DNA methylation, impact gene expression variability in metastable epialleles, affecting phenotype.

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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

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Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
07:26

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

Area of Science:

  • Epigenetics
  • Molecular Biology
  • Genomics

Background:

  • Environmental factors shape health and disease through epigenetic mechanisms mediating gene-environment interactions.
  • Metastable epialleles exhibit variable gene expression in genetically identical individuals due to epigenetic modifications during development.
  • While DNA methylation's role in metastable epialleles is known, histone modifications' influence remains largely unexplored.

Purpose of the Study:

  • To investigate the role of histone modifications in metastable epiallele expression and phenotypic variation.
  • To determine if histone patterns differ between mice with distinct metastable epiallele methylation states.
  • To understand how DNA and histone modifications interact to regulate gene expression.

Main Methods:

  • Chromatin immunoprecipitation followed by quantitative PCR (ChIP-qPCR) was used to analyze histone modifications.
  • The 5' long terminal repeat (LTR) of the murine viable yellow agouti (A(vy)) metastable epiallele was targeted.
  • CpG site methylation and specific histone marks (H3/H4 di-acetylation, H4K20 tri-methylation, H3K4 tri-methylation) were assessed.

Main Results:

  • Variable histone patterns were observed at the A(vy) LTR in isogenic mice.
  • Hypomethylated A(vy) LTR (yellow mice) showed enrichment of H3 and H4 di-acetylation.
  • Hypermethylated A(vy) LTR (pseudoagouti mice) showed enrichment of H4K20 tri-methylation; H3K4 tri-methylation showed no difference.

Conclusions:

  • Histone modifications, specifically di-acetylation and H4K20 tri-methylation, are associated with variable DNA methylation states at the A(vy) metastable epiallele.
  • DNA methylation acts in concert with histone modifications to regulate inter-individual variation in metastable epiallele expression.
  • Environmental epigenomic studies should consider the influence of environmental factors on histone modifications, not solely DNA methylation.