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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
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Riboswitches are RNA elements that regulate gene expression by altering their secondary structures in response to specific effector molecules. These elements, located in the leader regions of certain mRNAs, act as transcriptional regulators by toggling between alternative conformations to control downstream gene expression. Riboswitch-mediated regulation is a precise mechanism for modulating biosynthetic pathways, as exemplified by the riboflavin biosynthesis pathway in Bacillus...
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RNF138 joins the HR team.

Simon Bekker-Jensen1, Niels Mailand1

  • 1Ubiquitin Signaling Group, The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.

Nature Cell Biology
|October 31, 2015
PubMed
Summary

The E3 ubiquitin ligase RNF138 promotes DNA repair by aiding in DNA-end resection and homologous recombination. This discovery sheds light on how cells choose DNA repair pathways after double-strand breaks.

Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • DNA double-strand breaks (DSBs) are severe DNA damage.
  • Accurate repair of DSBs is crucial for maintaining genomic stability.
  • Cells employ complex mechanisms to choose between different DSB repair pathways.

Purpose of the Study:

  • To investigate the role of the E3 ubiquitin ligase RNF138 in DNA double-strand break repair.
  • To elucidate the molecular mechanisms by which RNF138 influences DSB repair pathway choice.

Main Methods:

  • Recruitment assays to DNA double-strand break sites.
  • Ubiquitylation assays of key DNA repair factors.
  • Analysis of homologous recombination and DNA-end resection.

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Main Results:

  • RNF138 is recruited to sites of DNA double-strand breaks.
  • RNF138 ubiquitylates essential DNA repair factors.
  • RNF138 promotes DNA-end resection and homologous recombination.

Conclusions:

  • RNF138 plays a critical role in promoting homologous recombination repair.
  • RNF138 functions by ubiquitylating repair factors at DSB sites.
  • These findings contribute to understanding the regulation of DNA repair pathway choice.