4.7 Article

Mgs1 protein supports genome stability via recognition of G-quadruplex DNA structures

期刊

FASEB JOURNAL
卷 34, 期 9, 页码 12646-12662

出版社

WILEY
DOI: 10.1096/fj.202000886R

关键词

DNA replication; genome stability; G-quadruplex; helicase; protein-DNA interaction

资金

  1. Emmy-Noether Program of the Deutsche Forschungsgemeinschaft
  2. EC | European Research Council (ERC) [638988-G4DSB]
  3. NSFC | National Natural Science Foundation of China-Yunnan Joint Fund (NSFC-Yunnan Joint Fund) [31700716]
  4. Nemzeti Kutatasi, Fejlesztesi es Innovacios Hivatal (NKFI Office) [119361, 116072, ERC_ HU117680, 123989]
  5. Eotvos Lorand Tudomanyegyetem (ELTE) [4.2.1/BOP 6072]

向作者/读者索取更多资源

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 theSaccharomyces cerevisiaeMgs1 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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