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

Alessio Magis, Silvia Götz, Mona Hajikazemi, Enikő Fekete-Szücs, Marco Caterino, Stefan Juranek and Katrin Paeschke ()
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Alessio Magis: University Hospital Bonn
Silvia Götz: University of Würzburg
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

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: 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.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17701-8

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DOI: 10.1038/s41467-020-17701-8

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