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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...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
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...

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Updated: Jun 24, 2026

Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
10:44

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Published on: January 31, 2018

Crosstalk between histone modifications during the DNA damage response.

Haico van Attikum1, Susan M Gasser

  • 1Department of Toxicogenetics, Leiden University Medical Center, Einthovenweg 20, 2333 ZC, Leiden, the Netherlands. h.van.attikum@lumc.nl

Trends in Cell Biology
|April 4, 2009
PubMed
Summary

Histone modifications like phosphorylation, acetylation, and ubiquitylation on H2AX at DNA double-strand breaks (DSBs) are crucial. These modifications regulate DNA repair factors and chromatin remodelers, preventing genomic instability.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Epigenetics

Background:

  • Chromatin structure is vital for cellular processes like DNA repair.
  • Histone variant H2AX is a key chromatin component involved in DNA double-strand break (DSB) response.
  • DSBs trigger rapid phosphorylation of H2AX.

Purpose of the Study:

  • To review how combined histone modifications at DSBs influence DNA repair.
  • To discuss the roles of specific histone modifications in recruiting DNA repair factors and chromatin remodelers.
  • To highlight the importance of these processes in maintaining genomic stability.

Main Methods:

  • Literature review of recent studies on histone modifications and DNA repair.
  • Analysis of the interplay between different histone marks (phosphorylation, acetylation, ubiquitylation).
  • Examination of the recruitment dynamics of DNA repair factors and chromatin remodeling complexes.

Main Results:

  • Specific combinations of histone modifications orchestrate the recruitment of DNA repair factors (e.g., MDC1, RNF8, RNF168, 53BP1, BRCA1).
  • These modifications also influence the assembly and function of chromatin remodeling complexes (e.g., INO80, SWR1, TIP60-p400).
  • The coordinated action of these factors at DSBs is essential for efficient repair and checkpoint control.

Conclusions:

  • Histone modifications on H2AX and surrounding chromatin are critical regulators of the DNA damage response.
  • The precise combinatorial code of modifications ensures proper recruitment and function of repair machinery.
  • This regulatory network prevents genomic instability and oncogenic transformation.