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Related Concept Videos

Histone Modification02:32

Histone Modification

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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...
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Spreading of Chromatin Modifications02:25

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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...
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DNA Damage can Stall the Cell Cycle02:37

DNA Damage can Stall the Cell Cycle

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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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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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....
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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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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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Nucleosome Remodeling02:54

Nucleosome Remodeling

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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.
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Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
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Histone post-translational modification and the DNA damage response.

Haoyun Song1, Rong Shen1, Xiangwen Liu1

  • 1School of Basic Medical Sciences, Lanzhou University, Lanzhou, Gansu 730000, China.

Genes & Diseases
|July 3, 2023
PubMed
Summary

DNA damage can lead to cancer if not repaired. Human cells use DNA damage response (DDR) mechanisms, involving histone post-translational modifications (PTMs), to maintain genome integrity and repair DNA damage.

Keywords:
DNA damageDNA damage responseHistonePost-translational modifications (PTMs)

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • DNA is constantly exposed to damage from internal and external sources.
  • Unrepaired DNA damage can cause genetic instability and elevate cancer risk.
  • Human cells have evolved sophisticated DNA damage response (DDR) pathways to protect genomic integrity.

Purpose of the Study:

  • To review the role of histone post-translational modifications (PTMs) in DNA damage repair.
  • To elucidate how histone PTMs facilitate the recruitment of DNA repair proteins.
  • To highlight emerging PTMs like succinylation and crotonylation in DNA repair.

Main Methods:

  • Literature review of studies on DNA damage repair mechanisms.
  • Analysis of the role of various histone modifications in response to DNA damage.
  • Examination of the functional impact of novel histone PTMs in DNA repair.

Main Results:

  • Histone PTMs are crucial regulators of DNA damage response pathways.
  • Specific histone PTMs modulate the recruitment and activity of DNA repair factors.
  • New histone modifications, including succinylation and crotonylation, are implicated in DNA repair processes.

Conclusions:

  • Understanding histone PTMs in DNA repair is vital for cancer therapy development.
  • Targeting DDR pathways involving histone PTMs may offer novel therapeutic strategies for cancer.
  • Further research into novel histone PTMs can uncover new avenues for cancer treatment.