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http://purl.uniprot.org/citations/28368371http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28368371http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28368371http://www.w3.org/2000/01/rdf-schema#comment"Replisome disassembly is the final step of DNA replication in eukaryotes, involving the ubiquitylation and CDC48-dependent dissolution of the CMG helicase (CDC45-MCM-GINS). Using Caenorhabditis elegans early embryos and Xenopus laevis egg extracts, we show that the E3 ligase CUL-2LRR-1 associates with the replisome and drives ubiquitylation and disassembly of CMG, together with the CDC-48 cofactors UFD-1 and NPL-4. Removal of CMG from chromatin in frog egg extracts requires CUL2 neddylation, and our data identify chromatin recruitment of CUL2LRR1 as a key regulated step during DNA replication termination. Interestingly, however, CMG persists on chromatin until prophase in worms that lack CUL-2LRR-1, but is then removed by a mitotic pathway that requires the CDC-48 cofactor UBXN-3, orthologous to the human tumour suppressor FAF1. Partial inactivation of lrr-1 and ubxn-3 leads to synthetic lethality, suggesting future approaches by which a deeper understanding of CMG disassembly in metazoa could be exploited therapeutically."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.org/dc/terms/identifier"doi:10.1038/ncb3500"xsd:string
http://purl.uniprot.org/citations/28368371http://purl.org/dc/terms/identifier"doi:10.1038/ncb3500"xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Johnson C."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Johnson C."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Hastie C.J."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Hastie C.J."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Gartner A."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Gartner A."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Sonneville R."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Sonneville R."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Knebel A."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Knebel A."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Labib K."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Labib K."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Gambus A."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Gambus A."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Moreno S.P."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/author"Moreno S.P."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/28368371http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string