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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...
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...
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 16, 2026

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

HDAC8 substrates: Histones and beyond.

Noah A Wolfson1, Carol Ann Pitcairn, Carol A Fierke

  • 1Department of Biological Chemistry, University of Michigan, Ann Arbor, MI.

Biopolymers
|November 24, 2012
PubMed
Summary
This summary is machine-generated.

Histone deacetylases (HDACs) remove acetyl groups from proteins. This review explores factors influencing HDAC8 substrate identification, crucial for understanding enzyme function.

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Last Updated: May 16, 2026

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

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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:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Histone deacetylases (HDACs) are enzymes catalyzing the removal of acetyl groups from lysine residues.
  • While initially known for histone deacetylation, HDACs also target numerous non-histone proteins.
  • Identifying specific HDAC substrates in vivo remains a significant challenge.

Purpose of the Study:

  • To review factors governing HDAC8 substrate recognition and catalytic activity.
  • To highlight the difficulties in identifying in vivo substrates for HDAC8.
  • To provide a framework for predicting HDAC substrate specificity.

Main Methods:

  • Literature review of existing studies on HDACs and HDAC8.
  • Analysis of structural and functional data related to HDAC8.
  • Discussion of in vivo, in vitro, and in silico approaches for substrate identification.

Main Results:

  • Thousands of acetylated proteins have been identified, but their specific deacetylases are often unknown.
  • HDAC8 is the most well-characterized HDAC kinetically and structurally.
  • Few efficient in vivo substrates for HDAC8 have been confirmed.

Conclusions:

  • Substrate recognition by HDAC8 is influenced by its structure, protein complex formation, and post-translational modifications.
  • Overcoming challenges in HDAC substrate identification requires integrated approaches.
  • Understanding these variables is key to predicting HDAC substrate specificity.