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SLX4 interacts with RTEL1 to prevent transcription-mediated DNA replication perturbations

A. Takedachi, E. Despras, S. Scaglione, R. Guérois, JH. Guervilly, M. Blin, S. Audebert, L. Camoin, Z. Hasanova, M. Schertzer, A. Guille, D. Churikov, I. Callebaut, V. Naim, M. Chaffanet, JP. Borg, F. Bertucci, P. Revy, D. Birnbaum, A....

. 2020 ; 27 (5) : 438-449. [pub] 20200511

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc20028218
E-zdroje Online Plný text

NLK ProQuest Central od 2004-01-01 do Před 1 rokem
Health & Medicine (ProQuest) od 2004-01-01 do Před 1 rokem

Odkazy

PubMed 32398829
DOI 10.1038/s41594-020-0419-3
Knihovny.cz E-zdroje

The SLX4 tumor suppressor is a scaffold that plays a pivotal role in several aspects of genome protection, including homologous recombination, interstrand DNA crosslink repair and the maintenance of common fragile sites and telomeres. Here, we unravel an unexpected direct interaction between SLX4 and the DNA helicase RTEL1, which, until now, were viewed as having independent and antagonistic functions. We identify cancer and Hoyeraal-Hreidarsson syndrome-associated mutations in SLX4 and RTEL1, respectively, that abolish SLX4-RTEL1 complex formation. We show that both proteins are recruited to nascent DNA, tightly co-localize with active RNA pol II, and that SLX4, in complex with RTEL1, promotes FANCD2/RNA pol II co-localization. Importantly, disrupting the SLX4-RTEL1 interaction leads to DNA replication defects in unstressed cells, which are rescued by inhibiting transcription. Our data demonstrate that SLX4 and RTEL1 interact to prevent replication-transcription conflicts and provide evidence that this is independent of the nuclease scaffold function of SLX4.

Citace poskytuje Crossref.org

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