Dbl2 interacts with helicases and an endonuclease to maintain the integrity of repetitive regions
Jazyk angličtina Země Velká Británie, Anglie Médium electronic
Typ dokumentu časopisecké články
Grantová podpora
APVV-20-0141
the Slovak Research and Development Agency
APVV-22-0294
the Slovak Research and Development Agency
AP0171
DoktoGrant
2/0021/22
the Slovak Grant Agency VEGA
1/0340/23
the Slovak Grant Agency VEGA
GAUK 248120
the Grant Agency of Charles University
GA23-05284S
the Czech Science Foundation grant
grant P30516
the Austrian Science Fund (FWF)
PubMed
40594858
PubMed Central
PMC12217596
DOI
10.1038/s41598-025-08626-7
PII: 10.1038/s41598-025-08626-7
Knihovny.cz E-zdroje
- Klíčová slova
- Schizosaccharomyces pombe, DNA repair, Dbl2, Helicases, Homologous recombination,
- MeSH
- DNA fungální metabolismus genetika MeSH
- DNA vazebné proteiny metabolismus MeSH
- DNA-helikasy * metabolismus genetika MeSH
- endonukleasy * metabolismus genetika MeSH
- poškození DNA MeSH
- repetitivní sekvence nukleových kyselin * MeSH
- replikace DNA MeSH
- Schizosaccharomyces pombe - proteiny * metabolismus genetika MeSH
- Schizosaccharomyces * genetika metabolismus MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- DNA fungální MeSH
- DNA vazebné proteiny MeSH
- DNA-helikasy * MeSH
- endonukleasy * MeSH
- Schizosaccharomyces pombe - proteiny * MeSH
Helicases and endonucleases play crucial roles in genome maintenance by unwinding or cleaving various forms of DNA and RNA structures in order to facilitate essential biological processes, such as DNA replication and recombination. Here, we identified fission yeast Dbl2 as a potential interactor of several complexes that exhibit either helicase or endonuclease activity, namely Fml1-MHF, SCFFbh1, Rqh1-Top3-Rmi1, and Mus81-Eme1. In vitro, Dbl2 binds to DNA, with a preference for branched molecules, such as D-loops, mobile Holliday junctions, and fork structures, making it a good candidate to play a central role in modulating the activity of helicases and endonucleases during replication and recombination repair. Previously, we showed that Dbl2 recruits Fbh1 to the ongoing homologous recombination sites, affecting the Rad51-nucleofilament. In this study, we determined that deleting dbl2 in an fbh1Δ background did not increase sensitivity to DNA-damaging agents or the frequency of Tf2 ectopic recombination. Therefore, Dbl2 and Fbh1 might be involved in the same molecular pathway, maintaining genome integrity by hindering ectopic recombination at repetitive elements.
Department of Biology Faculty of Medicine Masaryk University Kamenice 5 Brno 625 00 Czechia
Department of Cell Biology Faculty of Science Charles University 128 00 Praha 2 Czechia
Institute of Biochemistry and Biophysics Polish Academy of Sciences 02 106 Warsaw Poland
Institute of Chemistry Slovak Academy of Sciences Dubravska Cesta 9 845 38 Bratislava Slovakia
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