{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Thomas C"],"funding":["Rhode Island IDeA Networks of Biomedical Research Excellence","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["e0321886"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12040184"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(4)"],"pubmed_abstract":["DNA Polymerase Theta (Pol θ) is a conserved an A-family polymerase that plays an essential role in repairing double strand breaks, through micro-homology end joining, and bypassing DNA lesions, through translesion synthesis, to protect genome integrity. Despite its essential role in DNA repair, Pol θ is inherently error-prone. Recently, key loop regions were identified to play an important role in key functions of Pol θ. Here we present a comparative structure-function study of the polymerase domain of zebrafish and human Pol θ. We show that these two proteins share a large amount of sequence and structural homology. Using a classical biochemical approach we observe that zebrafish Pol θ displays behavior characteristic of human Pol θ, including DNA template extension in the presence of dif"],"journal":["PloS one"],"pubmed_title":["Zebrafish Polymerase Theta and human Polymerase Theta: Orthologues with homologous function."],"pmcid":["PMC12040184"],"funding_grant_id":["P20GM103430","R15GM144903-01","P20 GM103430","R15 GM144903"],"pubmed_authors":["Towle-Weicksel JB","Thomas C","Green S","Kimball L","Schmidtke IR","Weicksel SE","Griffin M","Palacio Y","Rothwell L","Par I","Schobel S"],"additional_accession":[]},"is_claimable":false,"name":"Zebrafish Polymerase Theta and human Polymerase Theta: Orthologues with homologous function.","description":"DNA Polymerase Theta (Pol θ) is a conserved an A-family polymerase that plays an essential role in repairing double strand breaks, through micro-homology end joining, and bypassing DNA lesions, through translesion synthesis, to protect genome integrity. Despite its essential role in DNA repair, Pol θ is inherently error-prone. Recently, key loop regions were identified to play an important role in key functions of Pol θ. Here we present a comparative structure-function study of the polymerase domain of zebrafish and human Pol θ. We show that these two proteins share a large amount of sequence and structural homology. Using a classical biochemical approach we observe that zebrafish Pol θ displays behavior characteristic of human Pol θ, including DNA template extension in the presence of dif","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025","modification":"2026-06-01T10:17:42.176Z","creation":"2025-07-10T03:09:11.465Z"},"accession":"S-EPMC12040184","cross_references":{"pubmed":["40299938"],"doi":["10.1371/journal.pone.0321886"]}}