2025
Dbl2 interacts with helicases and an endonuclease to maintain the integrity of repetitive regions
BAKOSOVA, Anetta; Lubos CIPAK; Nina MAYEROVA; Kamil KROL; Zsigmond BENKO et. al.Basic information
Original name
Dbl2 interacts with helicases and an endonuclease to maintain the integrity of repetitive regions
Authors
BAKOSOVA, Anetta; Lubos CIPAK; Nina MAYEROVA; Kamil KROL; Zsigmond BENKO; Alexandra PITELOVA; Peter KOLESÁR (703 Slovakia, belonging to the institution); Dominika PIATROVA; Maria SMONDRKOVA; Anna MARESOVA; Lucia MOLNAROVA; Ingrid CIPAKOVA; Veronika ALTMANNOVÁ (203 Czech Republic, belonging to the institution); Jana BELLOVA; Peter BARATH; Martin PREVOROVSKY; Jan PALEČEK (203 Czech Republic, belonging to the institution); Lumír KREJČÍ (203 Czech Republic, belonging to the institution); Juraj GREGAN; Adrianna SKONECZNA and Silvia BAGELOVA POLAKOVA
Edition
Scientific Reports, Berlin, NATURE RESEARCH, 2025, 2045-2322
Other information
Language
English
Type of outcome
Article in a journal
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
Germany
Confidentiality degree
is not subject to a state or trade secret
References:
Impact factor
Impact factor: 3.900 in 2024
Organization unit
Faculty of Medicine
UT WoS
001522988900028
EID Scopus
2-s2.0-105009533605
Keywords in English
Schizosaccharomyces pombe; DNA repair; Homologous recombination; Dbl2; Helicases
Tags
Tags
International impact, Reviewed
Changed: 8/8/2025 08:09, Mgr. Tereza Miškechová
Abstract
In the original language
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 fbh1 Delta 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.
Links
GA23-05284S, research and development project |
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