Timely lagging strand maturation relies on Ubp10 deubiquitylase-mediated PCNA dissociation from replicating chromatin

Javier Zamarreño, Sofía Muñoz, Esmeralda Alonso-Rodríguez, Macarena Alcalá, Sergio Rodríguez, Rodrigo Bermejo, María P. Sacristán () and Avelino Bueno ()
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Javier Zamarreño: Campus Miguel de Unamuno
Sofía Muñoz: Campus Miguel de Unamuno
Esmeralda Alonso-Rodríguez: Campus Miguel de Unamuno
Macarena Alcalá: Campus Miguel de Unamuno
Sergio Rodríguez: Campus Miguel de Unamuno
Rodrigo Bermejo: CSIC
María P. Sacristán: Campus Miguel de Unamuno
Avelino Bueno: Campus Miguel de Unamuno

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract Synthesis and maturation of Okazaki Fragments is an incessant and highly efficient metabolic process completing the synthesis of the lagging strands at replication forks during S phase. Accurate Okazaki fragment maturation (OFM) is crucial to maintain genome integrity and, therefore, cell survival in all living organisms. In eukaryotes, OFM involves the consecutive action of DNA polymerase Pol ∂, 5’ Flap endonuclease Fen1 and DNA ligase I, and constitutes the best example of a sequential process coordinated by the sliding clamp PCNA. For OFM to occur efficiently, cooperation of these enzymes with PCNA must be highly regulated. Here, we present evidence of a role for the K164-PCNA-deubiquitylase Ubp10 in the maturation of Okazaki fragments in the budding yeast Saccharomyces cerevisiae. We show that Ubp10 associates with lagging-strand DNA synthesis machineries on replicating chromatin to ensure timely ligation of Okazaki fragments by promoting PCNA dissociation from chromatin requiring lysine 164 deubiquitylation.

Date: 2024
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DOI: 10.1038/s41467-024-52542-9

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