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http://purl.uniprot.org/citations/28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28077247http://www.w3.org/2000/01/rdf-schema#comment"In 2003, we reported that 129-derived strains of mice carry a naturally occurring nonsense mutation at codon 27 of the Poli gene that would produce a polι peptide of just 26 amino acids, rather then the full-length 717 amino acid wild-type polymerase. In support of the genomic analysis, no polι protein was detected in testes extracts from 129X1/SvJmice, where wild-type polι is normally highly expressed. The early truncation in polι occurs before any structural domains of the polymerase are synthesized and as a consequence, we reasoned that 129-derived strains of mice should be considered as functionally defective in polι activity. However, it has recently been reported that during the maturation of the Poli mRNA in 129-derived strains, exon-2 is sometimes skipped and that an exon-2-less polι protein of 675 amino acids is synthesized that retains catalytic activity in vitro and in vivo. From a structural perspective, we found this idea untenable, given that the amino acids encoded by exon-2 include residues critical for the coordination of the metal ions required for catalysis, as well as the structural integrity of the DNA polymerase. To determine if the exon-2-less polι isoform possesses catalytic activity in vitro, we have purified a glutathione-tagged full-length exon-2-less (675 amino acid) polι protein from baculovirus infected insect cells and compared the activity of the isoform to full-length (717 amino acid) GST-tagged wild-type mouse polι in vitro. Reaction conditions were performed under a range of magnesium or manganese concentrations, as well as different template sequence contexts. Wild-type mouse polι exhibited robust characteristic properties previously associated with human polι's biochemical properties. However, we did not detect any polymerase activity associated with the exon-2-less polι enzyme under the same reaction conditions and conclude that exon-2-less polι is indeed rendered catalytically inactive in vitro."xsd:string
http://purl.uniprot.org/citations/28077247http://purl.org/dc/terms/identifier"doi:10.1016/j.dnarep.2016.12.004"xsd:string
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/author"McDonald J.P."xsd:string
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/author"Woodgate R."xsd:string
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/author"Yang W."xsd:string
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/author"Frank E.G."xsd:string
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/name"DNA Repair (Amst)"xsd:string
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/pages"71-76"xsd:string
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/title"Mouse DNA polymerase iota lacking the forty-two amino acids encoded by exon-2 is catalytically inactive in vitro."xsd:string
http://purl.uniprot.org/citations/28077247http://purl.uniprot.org/core/volume"50"xsd:string
http://purl.uniprot.org/citations/28077247http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28077247
http://purl.uniprot.org/citations/28077247http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28077247
http://purl.uniprot.org/uniprot/#_A0A0R4J1Z5-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_G8DM21-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_G8DM24-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_G8DM25-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_G8DM28-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_E9QJU6-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_E9Q3H9-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_Q7TNX7-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_Q6R3M4-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_Q3TQ92-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247
http://purl.uniprot.org/uniprot/#_Q8CF26-mappedCitation-28077247http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28077247