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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,...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
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...

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Related Experiment Video

Updated: Jun 4, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
10:40

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Histone H2A.Z acid patch residues required for deposition and function.

Kurt Jensen1, Maria Soledad Santisteban, Craig Urekar

  • 1Department of Microbiology, University of Virginia Health System, University of Virginia, P.O. Box 800734, Charlottesville, VA 22908-0734, USA. kurt.jensen@neurology.ufl.edu

Molecular Genetics and Genomics : MGG
|March 2, 2011
PubMed
Summary

The acidic patch of histone variant H2A.Z is crucial for its function and deposition into chromatin. Mutations in this region impair H2A.Z

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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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Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

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Analysis of Histone Antibody Specificity with Peptide Microarrays
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Analysis of Histone Antibody Specificity with Peptide Microarrays

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Last Updated: Jun 4, 2026

Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA
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Assembly of Nucleosomal Arrays from Recombinant Core Histones and Nucleosome Positioning DNA

Published on: September 10, 2013

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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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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Analysis of Histone Antibody Specificity with Peptide Microarrays
09:47

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Histone variants, like H2A.Z, dynamically alter chromatin structure.
  • The SWR1 complex facilitates H2A.Z incorporation, but target molecule requirements are unclear.

Purpose of the Study:

  • To identify key residues in H2A.Z essential for its function and chromatin deposition.
  • To understand the molecular mechanisms governing H2A.Z's role in chromatin regulation.

Main Methods:

  • Unbiased mutagenic screening in Saccharomyces cerevisiae.
  • Characterization of H2A.Z point mutations (htz1-D99A, htz1-D99K, htz1-E101K).
  • Phenotypic analysis under various growth conditions and chromatin immunoprecipitation (ChIP).

Main Results:

  • Specific acidic patch residues of H2A.Z are critical for its function.
  • Mutations in the acidic patch lead to functional defects and reduced protein levels.
  • Mutant H2A.Z variants show decreased detectability via ChIP at the PHO5 gene.

Conclusions:

  • Acidic patch residues mediate H2A.Z deposition and function within chromatin.
  • These residues are potential interaction sites for H2A.Z deposition and targeting machinery.
  • Understanding these interactions is key to elucidating chromatin remodeling mechanisms.