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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,...
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...
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...
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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Related Experiment Video

Updated: May 8, 2026

An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation
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An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation

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Probing the acetylation code of histone H4.

Diana Lang1, Michael Schümann, Kathy Gelato

  • 1Laboratory of Mass Spectrometry, Leibniz-Institut für Molekulare Pharmakologie, Berlin, Germany.

Proteomics
|August 24, 2013
PubMed
Summary

Histone H4 acetylation state cumulatively regulates genome function. Proteome-wide studies reveal that only fully acetylated H4 tails bind proteins, not specific acetylation sites.

Keywords:
Cell biologyChromatinHistone acetylationInteractome analysisQuantitative mass spectrometrySILAC

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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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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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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 and molecular biology
  • Genomic regulation
  • Post-translational modifications

Background:

  • Histone modifications, particularly lysine acetylation, are vital for genome regulation and transcriptional control.
  • The N-terminal tail of histone H4 is a key regulatory region.
  • Understanding acetylation-dependent interactions is crucial for deciphering gene expression mechanisms.

Purpose of the Study:

  • To conduct a proteome-wide investigation of protein-protein interactions mediated by the acetylated N-terminal tail of histone H4.
  • To identify proteins that bind to histone H4 tails with varying degrees of acetylation (mono-, bis-, triple-, and tetra-acetylation).

Main Methods:

  • Quantitative peptide-based affinity mass spectrometry (MS) experiments.
  • Stable Isotope Labeling by Amino acids in Cell culture (SILAC) approach for quantitative interactome analysis.
  • Analysis of H4 tails acetylated at specific sites (K5, K8, K12, K16) and combinations thereof.

Main Results:

  • A total of 29 proteins were found to be enriched on the fully tetra-acetylated H4 tail.
  • Specific protein binders for mono- and bis-acetylated H4 tails were largely undetectable.
  • The binding of proteins to H4 tails appears to be dependent on the cumulative acetylation state.

Conclusions:

  • The regulatory effects of histone H4 acetylation are established in a cumulative manner.
  • Protein recruitment is not driven by specific acetylation sites but rather by the overall pattern of acetylation on the H4 tail.
  • This finding supports a model where the degree of H4 acetylation dictates its interaction partners and regulatory functions.