{"database":"biostudies-other","file_versions":[],"scores":null,"additional":{"submitter":["Bunz F"],"funding":["NCI NIH HHS"],"pagination":["11014-8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC47912"],"abstract":["Replication factor C (RFC) is a multisubunit, DNA polymerase accessory protein required for the coordinated synthesis of both DNA strands during simian virus 40 DNA replication in vitro. Previous studies have shown that RFC is a DNA-dependent ATPase that binds in a structure-specific manner to the 3' end of a primer hybridized to a template DNA, an activity thought intrinsic to the 140-kDa component of this multisubunit complex. Here, the isolation and analysis of cDNAs encoding this subunit is described. Analysis of the full-length coding sequence revealed an open reading frame of 3.4 kb, encoding an 1148-amino acid protein with a predicted molecular mass of 130 kDa. A putative ATP-binding motif was observed that is similar to a motif in several of the smaller subunits of RFC and in functionally homologous replication factors of bacterial and viral origin. A \"DEAD\" box is also conserved among these proteins. The predicted protein shows significant identity with a DNA-binding protein of murine origin (B. Luckow, P. Lichter, and G. Schütz, personal communication). Regions of similarity were also seen between the amino acid sequences of the 140-kDa subunit of RFC, poly(ADP-ribose) polymerase, and bacterial DNA ligases--possibly representing a conserved structural feature of these proteins that bind similar DNA substrates."],"repository":["biostudies-other"],"data_source":["Europe PMC"],"omics_type":["Unknown"],"volume":["90(23)"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pmcid":["PMC47912"],"funding_grant_id":["CA13106"],"pubmed_authors":["Bunz F","Kobayashi R","Stillman B"],"additional_accession":[]},"is_claimable":false,"name":"cDNAs encoding the large subunit of human replication factor C.","description":"Replication factor C (RFC) is a multisubunit, DNA polymerase accessory protein required for the coordinated synthesis of both DNA strands during simian virus 40 DNA replication in vitro. Previous studies have shown that RFC is a DNA-dependent ATPase that binds in a structure-specific manner to the 3' end of a primer hybridized to a template DNA, an activity thought intrinsic to the 140-kDa component of this multisubunit complex. Here, the isolation and analysis of cDNAs encoding this subunit is described. Analysis of the full-length coding sequence revealed an open reading frame of 3.4 kb, encoding an 1148-amino acid protein with a predicted molecular mass of 130 kDa. A putative ATP-binding motif was observed that is similar to a motif in several of the smaller subunits of RFC and in functionally homologous replication factors of bacterial and viral origin. A \"DEAD\" box is also conserved among these proteins. The predicted protein shows significant identity with a DNA-binding protein of murine origin (B. Luckow, P. Lichter, and G. Schütz, personal communication). Regions of similarity were also seen between the amino acid sequences of the 140-kDa subunit of RFC, poly(ADP-ribose) polymerase, and bacterial DNA ligases--possibly representing a conserved structural feature of these proteins that bind similar DNA substrates.","dates":{"release":"1993-01-01T00:00:00Z","publication":"1993 Dec","modification":"2019-03-27T00:18:08Z","creation":"2019-03-27T00:18:08Z"},"accession":"S-EPMC47912","cross_references":{"gen":["L17340","L23320"],"pubmed":["8248204"],"doi":["10.1073/pnas.90.23.11014 "]}}