Related Experiment Video
Updated: Mar 15, 2026
10:12
Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
Published on: April 21, 2023
3.8K
Controlling DNA-End Resection: An Emerging Task for Ubiquitin and SUMO
Sarah-Felicitas Himmels1, Alessandro A Sartori1
1Institute of Molecular Cancer Research, University of Zurich Zurich, Switzerland.
Frontiers in Genetics
|September 8, 2016
Summary
Ubiquitylation and sumoylation regulate DNA double-strand break (DSB) repair by controlling DNA-end resection. These post-translational modifications are crucial for maintaining genomic stability and preventing cancer by directing repair pathway choice.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- DNA double-strand breaks (DSBs) are severe DNA lesions.
- Genomic instability resulting from improper DSB repair is a hallmark of cancer.
- Two main repair pathways, homologous recombination (HR) and non-homologous end joining (NHEJ), compete to repair DSBs.
Purpose of the Study:
- To provide a comprehensive overview of how ubiquitylation and sumoylation regulate DSB repair.
- To elucidate the role of these modifications in controlling the DNA-end resection machinery.
Main Methods:
- Literature review and synthesis of current research on ubiquitylation, sumoylation, and DSB repair.
- Analysis of the interplay between post-translational modifications and DNA repair pathways.
Main Results:
- Ubiquitylation and sumoylation are critical regulators of DNA damage signaling.
- These modifications modulate the DNA-end resection process, a key step in HR.
- By influencing resection, ubiquitylation and sumoylation impact the balance between HR and NHEJ.
Conclusions:
- Ubiquitylation and sumoylation are essential for accurate and efficient DSB repair.
- These modifications ensure genomic stability by directing DSBs to appropriate repair pathways.
- Targeting these regulatory mechanisms could offer new therapeutic strategies for cancer.
Related Concept Videos
01:08Nucleotide Excision Repair
41.6K
Overview
41.6K
01:38Nucleotide Excision Repair
5.6K
DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...
5.6K
02:53Conservative Site-specific Recombination and Phase Variation
7.3K
Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
The recognition sites for Cre recombinase called LoxP...
7.3K
01:13The Proteasome
1.9K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.9K
01:11Restriction Enzymes
38.0K
Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
38.0K
02:04Covalently Linked Protein Regulators
9.9K
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....
These groups modify specific amino acids in a protein....
9.9K