SUMO protease and proteasome recruitment at the nuclear periphery differently affect replication dynamics at arrested forks.

Autor:	Schirmeisen K; Institut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.; Université Paris-Saclay, CNRS UMR3348, 91400 Orsay, France., Naiman K; INSERM U1068, CNRS UMR7258, Aix Marseille Univ U105, Institut Paoli-Calmettes, CRCM, Marseille, France.; Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer BN1 9RQ, UK., Fréon K; Institut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.; Université Paris-Saclay, CNRS UMR3348, 91400 Orsay, France., Besse L; Institut Curie, Université PSL, CNRS UAR2016, Inserm US43, Université Paris-Saclay, Multimodal Imaging Center, 91400 Orsay, France., Chakraborty S; Institut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.; Université Paris-Saclay, CNRS UMR3348, 91400 Orsay, France., Saada AA; Institut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.; Université Paris-Saclay, CNRS UMR3348, 91400 Orsay, France., Carr AM; Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer BN1 9RQ, UK., Kramarz K; Academic Excellence Hub - Research Centre for DNA Repair and Replication, Faculty of Biological Sciences, University of Wroclaw, 50-328 Wroclaw, Poland., Lambert SAE; Institut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.; Université Paris-Saclay, CNRS UMR3348, 91400 Orsay, France.; Equipe Labellisée Ligue Nationale Contre le cancer, France.
Jazyk:	angličtina
Zdroj:	Nucleic acids research [Nucleic Acids Res] 2024 Aug 12; Vol. 52 (14), pp. 8286-8302.
DOI:	10.1093/nar/gkae526
Abstrakt:	Nuclear pore complexes (NPCs) have emerged as genome organizers, defining a particular nuclear compartment enriched for SUMO protease and proteasome activities, and act as docking sites for the repair of DNA damage. In fission yeast, the anchorage of perturbed replication forks to NPCs is an integral part of the recombination-dependent replication restart mechanism (RDR) that resumes DNA synthesis at terminally dysfunctional forks. By mapping DNA polymerase usage, we report that SUMO protease Ulp1-associated NPCs ensure efficient initiation of restarted DNA synthesis, whereas proteasome-associated NPCs sustain the progression of restarted DNA polymerase. In contrast to Ulp1-dependent events, this last function is not alleviated by preventing SUMO chain formation. By analyzing the role of the nuclear basket, the nucleoplasmic extension of the NPC, we reveal that the activities of Ulp1 and the proteasome cannot compensate for each other and affect the dynamics of RDR in distinct ways. Our work probes two distinct mechanisms by which the NPC environment ensures optimal RDR, both controlled by different NPC components. (© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Databáze:	MEDLINE
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