{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bjergbaek L"],"funding":["NCCDPHP CDC HHS"],"pagination":["405-17"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC545806"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["24(2)"],"pubmed_abstract":["The RecQ helicase Sgs1p forms a complex with the type 1 DNA topoisomerase Top3p that resolves double Holliday junctions resulting from Rad51-mediated exchange. We find, however, that Sgs1p functions independently of both Top3p and Rad51p to stimulate the checkpoint kinase Rad53p when replication forks stall due to dNTP depletion on hydroxyurea. Checkpoint activation does not require Sgs1p function as a helicase, and correlates with its ability to bind the Rad53p kinase FHA1 motif directly. On the other hand, Sgs1p's helicase activity is required together with Top3p and the strand-exchange factor Rad51p, to help stabilise DNA polymerase epsilon at stalled replication forks. In this function, the Sgs1p/Top3p complex acts in parallel to the Claspin-related adaptor, Mrc1p, although the sgs1 an"],"journal":["The EMBO journal"],"pubmed_title":["Mechanistically distinct roles for Sgs1p in checkpoint activation and replication fork maintenance."],"pmcid":["PMC545806"],"funding_grant_id":["U48 DP000060"],"pubmed_authors":["Bjergbaek L","Cobb JA","Tsai-Pflugfelder M","Gasser SM"],"additional_accession":[]},"is_claimable":false,"name":"Mechanistically distinct roles for Sgs1p in checkpoint activation and replication fork maintenance.","description":"The RecQ helicase Sgs1p forms a complex with the type 1 DNA topoisomerase Top3p that resolves double Holliday junctions resulting from Rad51-mediated exchange. We find, however, that Sgs1p functions independently of both Top3p and Rad51p to stimulate the checkpoint kinase Rad53p when replication forks stall due to dNTP depletion on hydroxyurea. Checkpoint activation does not require Sgs1p function as a helicase, and correlates with its ability to bind the Rad53p kinase FHA1 motif directly. On the other hand, Sgs1p's helicase activity is required together with Top3p and the strand-exchange factor Rad51p, to help stabilise DNA polymerase epsilon at stalled replication forks. In this function, the Sgs1p/Top3p complex acts in parallel to the Claspin-related adaptor, Mrc1p, although the sgs1 an","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005 Jan","modification":"2025-04-20T01:38:19.882Z","creation":"2019-03-27T01:08:32Z"},"accession":"S-EPMC545806","cross_references":{"pubmed":["15616582"],"doi":["10.1038/sj.emboj.7600511"]}}