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Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair

Author

Listed:
  • Alessio Magis

    (University Hospital Bonn)

  • Silvia Götz

    (University of Würzburg
    University of Groningen)

  • Mona Hajikazemi

    (University Hospital Bonn)

  • Enikő Fekete-Szücs

    (University of Groningen)

  • Marco Caterino

    (University Hospital Bonn)

  • Stefan Juranek

    (University Hospital Bonn)

  • Katrin Paeschke

    (University Hospital Bonn
    University of Würzburg
    University of Groningen)

Abstract

Nucleic acids can fold into G-quadruplex (G4) structures that can fine-tune biological processes. Proteins are required to recognize G4 structures and coordinate their function. Here we identify Zuo1 as a novel G4-binding protein in vitro and in vivo. In vivo in the absence of Zuo1 fewer G4 structures form, cell growth slows and cells become UV sensitive. Subsequent experiments reveal that these cellular changes are due to reduced levels of G4 structures. Zuo1 function at G4 structures results in the recruitment of nucleotide excision repair (NER) factors, which has a positive effect on genome stability. Cells lacking functional NER, as well as Zuo1, accumulate G4 structures, which become accessible to translesion synthesis. Our results suggest a model in which Zuo1 supports NER function and regulates the choice of the DNA repair pathway nearby G4 structures.

Suggested Citation

  • Alessio Magis & Silvia Götz & Mona Hajikazemi & Enikő Fekete-Szücs & Marco Caterino & Stefan Juranek & Katrin Paeschke, 2020. "Zuo1 supports G4 structure formation and directs repair toward nucleotide excision repair," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17701-8
    DOI: 10.1038/s41467-020-17701-8
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    Cited by:

    1. Alessio Magis & Michaela Limmer & Venkat Mudiyam & David Monchaud & Stefan Juranek & Katrin Paeschke, 2023. "UV-induced G4 DNA structures recruit ZRF1 which prevents UV-induced senescence," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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