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Mgs1 protein supports genome stability via recognition of G-quadruplex DNA structures.
Zacheja, Theresa; Toth, Agnes; Harami, Gabor M; Yang, Qianlu; Schwindt, Eike; Kovács, Mihály; Paeschke, Katrin; Burkovics, Peter.
Afiliação
  • Zacheja T; Department of Oncology, Hematology and Rheumatology, University Hospital Bonn, Bonn, Germany.
  • Toth A; Biological Research Centre, Institute of Genetics, Szeged, Hungary.
  • Harami GM; Doctoral School of Biology, Faculty of Science and Informatics, University of Szeged, Szeged, Hungary.
  • Yang Q; ELTE-MTA Momentum Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
  • Schwindt E; Department of Biochemistry, Biocenter, University of Wuerzburg, Wuerzburg, Germany.
  • Kovács M; Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Nanjing Medical University, Nanjing, China.
  • Paeschke K; Department of Oncology, Hematology and Rheumatology, University Hospital Bonn, Bonn, Germany.
  • Burkovics P; ELTE-MTA Momentum Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
FASEB J ; 34(9): 12646-12662, 2020 09.
Article em En | MEDLINE | ID: mdl-32748509
ABSTRACT
The integrity of the genetic material is crucial for every organism. One intrinsic attack to genome stability is stalling of the replication fork which can result in DNA breakage. Several factors, such as DNA lesions or the formation of stable secondary structures (eg, G-quadruplexes) can lead to replication fork stalling. G-quadruplexes (G4s) are well-characterized stable secondary DNA structures that can form within specific single-stranded DNA sequence motifs and have been shown to block/pause the replication machinery. In most genomes several helicases have been described to regulate G4 unfolding to preserve genome integrity, however, different experiments raise the hypothesis that processing of G4s during DNA replication is more complex and requires additional, so far unknown, proteins. Here, we show that the Saccharomyces cerevisiae Mgs1 protein robustly binds to G4 structures in vitro and preferentially acts at regions with a strong potential to form G4 structures in vivo. Our results suggest that Mgs1 binds to G4-forming sites and has a role in the maintenance of genome integrity.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / DNA Helicases / Proteínas de Saccharomyces cerevisiae / Instabilidade Genômica / Proteínas de Ligação a DNA / Quadruplex G Idioma: En Revista: FASEB J Assunto da revista: BIOLOGIA / FISIOLOGIA Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Saccharomyces cerevisiae / DNA Helicases / Proteínas de Saccharomyces cerevisiae / Instabilidade Genômica / Proteínas de Ligação a DNA / Quadruplex G Idioma: En Revista: FASEB J Assunto da revista: BIOLOGIA / FISIOLOGIA Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Alemanha
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