Reference - PMID:38917328 - SUMO protease and proteasome recruitment at the nuclear periphery differently affect replication dynamics at arrested forks.

Reference summary

PubMed ID

PMID:38917328

Title

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

Authors

Schirmeisen K, Naiman K, Fréon K, Besse L, Chakraborty S, Saada AA, Carr AM, Kramarz K, Lambert SAE

Citation

Nucleic Acids Res 2024 Jun 25;

Publication year

2024

Abstract

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.

Annotation