{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mikheikin AL"],"funding":["NIGMS NIH HHS"],"pagination":["7194-205"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2790891"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["37(21)"],"pubmed_abstract":["DNA polymerases are essential enzymes in all domains of life for both DNA replication and repair. The primary DNA replication polymerase from Sulfolobus solfataricus (SsoDpo1) has been shown previously to provide the necessary polymerization speed and exonuclease activity to replicate the genome accurately. We find that this polymerase is able to physically associate with itself to form a trimer and that this complex is stabilized in the presence of DNA. Analytical gel filtration and electrophoretic mobility shift assays establish that initially a single DNA polymerase binds to DNA followed by the cooperative binding of two additional molecules of the polymerase at higher concentrations of the enzyme. Protein chemical crosslinking experiments show that these are specific polymerase-polymer"],"journal":["Nucleic acids research"],"pubmed_title":["A trimeric DNA polymerase complex increases the native replication processivity."],"pmcid":["PMC2790891"],"funding_grant_id":["R37 GM029207","R01 GM029207","5R37GM029207"],"pubmed_authors":["Jen-Jacobson L","Mehta P","Lin HK","Mikheikin AL","Trakselis MA"],"additional_accession":[]},"is_claimable":false,"name":"A trimeric DNA polymerase complex increases the native replication processivity.","description":"DNA polymerases are essential enzymes in all domains of life for both DNA replication and repair. The primary DNA replication polymerase from Sulfolobus solfataricus (SsoDpo1) has been shown previously to provide the necessary polymerization speed and exonuclease activity to replicate the genome accurately. We find that this polymerase is able to physically associate with itself to form a trimer and that this complex is stabilized in the presence of DNA. Analytical gel filtration and electrophoretic mobility shift assays establish that initially a single DNA polymerase binds to DNA followed by the cooperative binding of two additional molecules of the polymerase at higher concentrations of the enzyme. Protein chemical crosslinking experiments show that these are specific polymerase-polymer","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Nov","modification":"2025-04-26T12:40:47.375Z","creation":"2019-03-27T00:27:17Z"},"accession":"S-EPMC2790891","cross_references":{"pubmed":["19773426"],"doi":["10.1093/nar/gkp767"]}}