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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...
DNA Damage Can Stall the Cell Cycle02:36

DNA Damage Can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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...

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Related Experiment Video

Updated: Jul 16, 2026

Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
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Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage

Published on: January 31, 2018

Histone modifications in response to DNA damage.

Mohammed Altaf1, Nehmé Saksouk, Jacques Côté

  • 1Laval University Cancer Research Center, Hôtel-Dieu de Québec, Quebec City, Quebec, Canada.

Mutation Research
|February 20, 2007
PubMed
Summary

Eukaryotic DNA repair relies on overcoming chromatin barriers. Histone modifications are crucial signals and platforms for DNA repair proteins, maintaining genome integrity.

Area of Science:

  • Molecular Biology
  • Genetics
  • Epigenetics

Background:

  • Eukaryotic genomes are packaged into condensed chromatin, restricting access for essential processes like transcription and DNA repair.
  • Complex mechanisms have evolved in eukaryotes to overcome chromatin's repressive nature.
  • Histone modifying enzymes and ATP-dependent chromatin remodelers are key players in regulating nuclear processes by altering chromatin structure.

Purpose of the Study:

  • To review recent advancements in understanding histone modifications.
  • To elucidate the role of histone modifications in maintaining genome integrity.
  • To highlight the significance of these modifications in DNA repair pathways.

Main Methods:

  • This is a review article, summarizing existing research.

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Proximity Ligand Assay to Localize Proteins in DNA Damage Sites
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Proximity Ligand Assay to Localize Proteins in DNA Damage Sites

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Proximity Ligand Assay to Localize Proteins in DNA Damage Sites
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Proximity Ligand Assay to Localize Proteins in DNA Damage Sites

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  • Focuses on analyzing literature concerning histone modifications and their impact on DNA repair.
  • Synthesizes findings on the signaling and scaffolding functions of histone modifications in genome maintenance.

    • Main Results:

    • Histone modifications act as critical signals and landing platforms for proteins involved in DNA repair.
    • These modifications are integral to the efficient execution of DNA repair processes.
    • The regulation of chromatin structure by histone modifications is essential for maintaining genome integrity.

    Conclusions:

    • Histone modifications play a vital role in facilitating DNA repair mechanisms.
    • Understanding these epigenetic marks is key to comprehending genome stability.
    • Continued research into histone modifications will advance our knowledge of nuclear processes and disease.