Dbl2 interacts with helicases and an endonuclease to maintain the integrity of repetitive regions

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F25%3A00144394" target="_blank" >RIV/00216224:14110/25:00144394 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/25:10514065

Výsledek na webu

<a href="https://www.nature.com/articles/s41598-025-08626-7" target="_blank" >https://www.nature.com/articles/s41598-025-08626-7</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41598-025-08626-7" target="_blank" >10.1038/s41598-025-08626-7</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Dbl2 interacts with helicases and an endonuclease to maintain the integrity of repetitive regions

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Dbl2 interacts with helicases and an endonuclease to maintain the integrity of repetitive regions

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA23-05284S" target="_blank" >GA23-05284S: Rozluštění vztahu mezi homologní rekombinací a umlčením genů</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Scientific Reports

ISSN

2045-2322

e-ISSN

—

Svazek periodika

15

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

18

Strana od-do

1-18

Kód UT WoS článku

001522988900028

EID výsledku v databázi Scopus

2-s2.0-105009533605