{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["287(12)"],"submitter":["Munashingha PR"],"pubmed_abstract":["Dna2 and Rad27 (yeast Fen1) are the two endonucleases critical for Okazaki fragment processing during lagging strand DNA synthesis that have been shown to interact genetically and physically. In this study, we addressed the functional consequences of these interactions by examining whether purified Rad27 of Saccharomyces cerevisiae affects the enzymatic activity of Dna2 and vice versa. For this purpose, we constructed Rad27DA (catalytically defective enzyme with an Asp to Ala substitution at amino acid 179) and found that it significantly stimulated the endonuclease activity of wild type Dna2, but failed to do so with Dna2Δ405N that lacks the N-terminal 405 amino acids. This was an unexpected finding because dna2Δ405N cells were still partially suppressed by overexpression of rad27DA in vi"],"journal":["The Journal of biological chemistry"],"pagination":["8675-87"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3308799"],"repository":["biostudies-literature"],"pubmed_title":["The trans-autostimulatory activity of Rad27 suppresses dna2 defects in Okazaki fragment processing."],"pmcid":["PMC3308799"],"pubmed_authors":["Lee CH","Munashingha PR","Kang YH","Seo YS","Shin YK","Nguyen TA"],"additional_accession":[]},"is_claimable":false,"name":"The trans-autostimulatory activity of Rad27 suppresses dna2 defects in Okazaki fragment processing.","description":"Dna2 and Rad27 (yeast Fen1) are the two endonucleases critical for Okazaki fragment processing during lagging strand DNA synthesis that have been shown to interact genetically and physically. In this study, we addressed the functional consequences of these interactions by examining whether purified Rad27 of Saccharomyces cerevisiae affects the enzymatic activity of Dna2 and vice versa. For this purpose, we constructed Rad27DA (catalytically defective enzyme with an Asp to Ala substitution at amino acid 179) and found that it significantly stimulated the endonuclease activity of wild type Dna2, but failed to do so with Dna2Δ405N that lacks the N-terminal 405 amino acids. This was an unexpected finding because dna2Δ405N cells were still partially suppressed by overexpression of rad27DA in vi","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Mar","modification":"2025-04-05T12:06:51.755Z","creation":"2019-03-27T00:51:25Z"},"accession":"S-EPMC3308799","cross_references":{"pubmed":["22235122"],"doi":["10.1074/jbc.M111.326470","10.1074/jbc.m111.326470"]}}