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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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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...

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Related Experiment Video

Updated: Jun 4, 2026

An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation
05:44

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

Published on: January 26, 2024

Histone acetylation and deacetylation.

K Ito1, P J Barnes, I M Adcock

  • 1National Heart and Lung Institute, Imperial College School of Medicine, London, UK.

Methods in Molecular Medicine
|February 12, 2011
PubMed
Summary
This summary is machine-generated.

Cellular DNA is packaged into chromatin, which normally blocks gene transcription. Post-translational modification of histone proteins, specifically acetylation, regulates DNA accessibility and gene expression, impacting cellular activation and function.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • DNA in resting cells is compacted into chromatin, limiting transcription factor access.
  • Chromatin's fundamental unit, the nucleosome, comprises histone proteins and DNA, acting as a barrier to transcription initiation.
  • Post-translational modification of histone N-terminal tails, particularly acetylation, influences DNA accessibility.

Purpose of the Study:

  • To investigate the role of histone acetylation in regulating gene transcription.
  • To explore the mechanisms by which histone acetyltransferase (HAT) and histone deacetylase (HDAC) enzymes control gene expression.

Main Methods:

  • The study focuses on the dynamic equilibrium of core histone acetylation.
  • It examines the enzymatic activities of histone acetyltransferase (HAT) and histone deacetylase (HDAC) in regulating transcription.
  • The research correlates histone acetylation levels with gene transcription rates.

Main Results:

  • Increased gene transcription is strongly associated with elevated levels of histone acetylation.
  • Conversely, hypoacetylation of histones correlates with reduced gene transcription and gene silencing.
  • Transcriptional regulators with intrinsic HAT and HDAC activities suggest a causal role for histone acetylation in transcription regulation.

Conclusions:

  • Histone acetylation is a critical epigenetic mechanism for regulating gene transcription.
  • The balance between HAT and HDAC activities is essential for controlling DNA accessibility and gene expression.
  • Understanding histone acetylation dynamics provides insights into cellular activation and gene regulation processes.