{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cho WH"],"funding":["PHS HHS","NIGMS NIH HHS"],"pagination":["2523-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3574903"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["110(7)"],"pubmed_abstract":["Tim (Timeless) and Tipin (Tim-interacting protein) form a stable heterodimeric complex that influences checkpoint responses and replication fork progression. We report that the Tim-Tipin complex interacts with essential replication fork proteins and affects their biochemical properties. The Tim-Tipin complex, reconstituted and purified using the baculovirus expression system, interacts directly with Mcm complexes and inhibits the single-stranded DNA-dependent ATPase activities of the Mcm2-7 and Mcm4/6/7 complexes, the DNA unwinding activity of the Mcm4/6/7 complex, and the DNA unwinding and ATPase activity of Cdc45-Mcm2-7-GINS complex, the presumed replicative DNA helicase in eukaryotes. Although stable interactions between Tim-Tipin and DNA polymerases (pols) were not observed in immunopr"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Human Tim-Tipin complex affects the biochemical properties of the replicative DNA helicase and DNA polymerases."],"pmcid":["PMC3574903"],"funding_grant_id":["R01 GM034559","GMS R01 GM034559"],"pubmed_authors":["Tappin I","An YY","Cho WH","Kang YH","Lee JK","Hurwitz J"],"additional_accession":[]},"is_claimable":false,"name":"Human Tim-Tipin complex affects the biochemical properties of the replicative DNA helicase and DNA polymerases.","description":"Tim (Timeless) and Tipin (Tim-interacting protein) form a stable heterodimeric complex that influences checkpoint responses and replication fork progression. We report that the Tim-Tipin complex interacts with essential replication fork proteins and affects their biochemical properties. The Tim-Tipin complex, reconstituted and purified using the baculovirus expression system, interacts directly with Mcm complexes and inhibits the single-stranded DNA-dependent ATPase activities of the Mcm2-7 and Mcm4/6/7 complexes, the DNA unwinding activity of the Mcm4/6/7 complex, and the DNA unwinding and ATPase activity of Cdc45-Mcm2-7-GINS complex, the presumed replicative DNA helicase in eukaryotes. Although stable interactions between Tim-Tipin and DNA polymerases (pols) were not observed in immunopr","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Feb","modification":"2025-04-26T08:55:04.156Z","creation":"2019-03-27T01:04:54Z"},"accession":"S-EPMC3574903","cross_references":{"pubmed":["23359676"],"doi":["10.1073/pnas.1222494110"]}}