The p97 segregase cofactor Ubxn7 facilitates replisome disassembly during S-phase.

ABSTRACT: Complex cellular processes are driven by the regulated assembly and disassembly of large multiprotein complexes. While we are beginning to understand the molecular mechanism for assembly of the eukaryotic DNA replication machinery (replisome), we still know relatively little about the regulation of its disassembly at replication termination. Recently, the first elements of this process have emerged, revealing that the replicative helicase, at the heart of the replisome, is polyubiquitylated prior to unloading and that this unloading requires p97 segregase activity. Two different E3 ubiquitin ligases have now been shown to ubiquitylate the helicase under different conditions: Cul2^Lrr1 and TRAIP. Here, using Xenopus laevis egg extract cell-free system and biochemical approaches, w

SUBMITTER: Tarcan Z 

PROVIDER: S-EPMC9358472 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature