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Related Concept Videos

DNA Damage Can Stall the Cell Cycle02:36

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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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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In order to be passed through generations, genomic DNA must be undamaged and error-free. However, every day, DNA in a cell undergoes several thousand to a million damaging events by natural causes and external factors. Ionizing radiation such as UV rays, free radicals produced during cellular respiration, and hydrolytic damage from metabolic reactions can alter the structure of DNA. Damages caused include single-base alteration, base dimerization, chain breaks, and cross-linkage.
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Translesion DNA Polymerases02:10

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Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
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DNA-only transposons are called autonomous transposons since they code for the enzyme transposase that is required for the transposition mechanism. Insertion of transposons can alter gene functions in multiple ways. They can mutate the gene, alter gene expression by introducing a novel promoter or insulator sequence, introduce new splice sites, and change the mRNA transcripts produced, or remodel chromatin structure.
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Related Experiment Video

Updated: Feb 1, 2026

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RNF126 Quenches RNF168 Function in the DNA Damage Response.

Lianzhong Zhang1, Zhenzhen Wang2, Ruifeng Shi3

  • 1College of Life Sciences, Capital Normal University, Beijing 100048, China; Faculty of Life Sciences, Tangshan Normal College, Tangshan 063000, China.

Genomics, Proteomics & Bioinformatics
|December 12, 2018
PubMed
Summary

Ring finger protein 126 (RNF126) negatively regulates DNA damage response (DDR) by inhibiting RNF168. Proper RNF126 levels are crucial for homologous recombination repair of DNA double-strand breaks.

Keywords:
DNA damage responseDNA repairRNF126RNF168RNF8Ubiquitination

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • DNA damage response (DDR) is critical for genome stability and preventing cancer.
  • Ubiquitin modifications are key regulators of DDR signaling and DNA repair pathways.

Purpose of the Study:

  • To investigate the role of E3 ligase RNF126 in the DNA damage response.
  • To elucidate the mechanism by which RNF126 influences DDR and DNA repair.

Main Methods:

  • Utilized UV laser micro-irradiation to induce DNA damage.
  • Investigated protein-protein interactions and ubiquitination events using co-immunoprecipitation and Western blotting.
  • Assessed DNA repair efficiency via homologous recombination assays and focus formation of DDR markers.

Main Results:

  • RNF126 is recruited to sites of DNA damage in a RNF8-dependent manner.
  • RNF126 directly interacts with and ubiquitinates E3 ligase RNF168.
  • RNF126 overexpression inhibits H2AX ubiquitination and downstream focus formation of 53BP1 and RAP80.
  • Both RNF126 overexpression and downregulation impair homologous recombination repair of DNA double-strand breaks.

Conclusions:

  • RNF126 acts as a negative regulator of RNF168 activity within the DDR pathway.
  • Maintaining appropriate cellular levels of RNF126 is essential for efficient homologous recombination-mediated repair of DNA double-strand breaks.