{"doi":"10.1073/pnas.90.19.9105","title":"DNA polymerase delta from embryos of Drosophila melanogaster.","abstract":"<jats:p>We have purified a DNA polymerase activity from 0- to 2-hr embryos of Drosophila melanogaster to near homogeneity. The purified enzyme consists of a single 120-kDa polypeptide, which contains polymerase and 3'--&gt;5' exonuclease activities. Exonuclease activity is inhibited by deoxynucleoside triphosphates, suggesting that the polymerase and exonuclease activities are coupled. The polymerase is more active with poly(dA-dT) than with activated DNA or poly(dA)/oligo(dT) as template. It shows a low degree of processivity with poly(dA)/oligo(dT). The polymerase is sensitive to aphidicolin and carbonyldiphosphonate but resistant to N2-[p-(n-butyl)phenyl]-2-deoxyguanosine triphosphate, 2-[p-(n-butyl)anilino]-2-deoxyadenosine triphosphate, and dideoxythymidine triphosphate. The 120-kDa polypeptide can be distinguished from the large subunit of Drosophila DNA polymerase alpha on the basis of the peptides generated by partial cleavage with N-chlorosuccinimide and by its failure to react with a monoclonal antibody directed against the large subunit of DNA polymerase alpha. The DNA polymerase is inhibited by 200 mM NaCl and is unable to use poly(rA)/oligo(dT) as a template, thus differentiating it from DNA polymerase gamma. On the basis of these properties, we propose that the DNA polymerase that we have purified from 0- to 2-hr Drosophila melanogaster embryos is DNA polymerase delta.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1993,"id":617974,"datarank":0.519860385419959,"base_score":3.4657359027997265,"endowment":3.4657359027997265,"self_citation_contribution":0.519860385419959,"citation_network_contribution":0.0,"self_endowment_contribution":0.519860385419959,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":31,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1593903,"name":"P G Mitsis","orcid":null,"position":1,"is_corresponding":false},{"id":1593904,"name":"I R Lehman","orcid":null,"position":2,"is_corresponding":false},{"id":1593902,"name":"C S Chiang","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"DNA polymerase delta from embryos of Drosophila melanogaster.","abstract":"<jats:p>We have purified a DNA polymerase activity from 0- to 2-hr embryos of Drosophila melanogaster to near homogeneity. The purified enzyme consists of a single 120-kDa polypeptide, which contains polymerase and 3'--&gt;5' exonuclease activities. Exonuclease activity is inhibited by deoxynucleoside triphosphates, suggesting that the polymerase and exonuclease activities are coupled. The polymerase is more active with poly(dA-dT) than with activated DNA or poly(dA)/oligo(dT) as template. It shows a low degree of processivity with poly(dA)/oligo(dT). The polymerase is sensitive to aphidicolin and carbonyldiphosphonate but resistant to N2-[p-(n-butyl)phenyl]-2-deoxyguanosine triphosphate, 2-[p-(n-butyl)anilino]-2-deoxyadenosine triphosphate, and dideoxythymidine triphosphate. The 120-kDa polypeptide can be distinguished from the large subunit of Drosophila DNA polymerase alpha on the basis of the peptides generated by partial cleavage with N-chlorosuccinimide and by its failure to react with a monoclonal antibody directed against the large subunit of DNA polymerase alpha. The DNA polymerase is inhibited by 200 mM NaCl and is unable to use poly(rA)/oligo(dT) as a template, thus differentiating it from DNA polymerase gamma. On the basis of these properties, we propose that the DNA polymerase that we have purified from 0- to 2-hr Drosophila melanogaster embryos is DNA polymerase delta.</jats:p>","is_dataset_classified":null,"base_score":3.4657359027997265,"endowment":3.4657359027997265,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"8415662","pmcid":"PMC47510","openalex_id":"https://openalex.org/W2064859373","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM-06196","title":null}],"total_grants":1,"fwci":1.4863,"citation_percentile":0.82357964,"influential_citations":0,"citation_trend":[{"year":2014,"count":1},{"year":2020,"count":1},{"year":2023,"count":2}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://pnas.org/doi/pdf/10.1073/pnas.90.19.9105","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.90.19.9105","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/8415662","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/47510","host_type":"repository"}],"fields_of_study":["DNA and Nucleic Acid Chemistry","DNA Repair Mechanisms","RNA Interference and Gene Delivery","Animals","Chromatography","Chromatography, Affinity","Chromatography, Ion Exchange","DNA Polymerase III","DNA-Directed DNA Polymerase","Drosophila melanogaster","Durapatite","Embryo, Nonmammalian","Kinetics","Macromolecular Substances","Molecular Weight","Peptide Mapping"],"mesh_terms":["Animals","Chromatography","Chromatography, Affinity","Chromatography, Ion Exchange","DNA Polymerase III","DNA-Directed DNA Polymerase","Drosophila melanogaster","Embryo, Nonmammalian","Kinetics","Molecular Weight","Peptide Mapping","Durapatite","Macromolecular Substances"],"keywords":["DNA polymerase","Polymerase","Molecular biology","DNA polymerase II","DNA clamp","Klenow fragment","DNA polymerase I","Biology","Exonuclease","DNA polymerase mu","Processivity","Biochemistry","DNA polymerase delta","DNA","Polymerase chain reaction","Reverse transcriptase","Circular bacterial chromosome","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-03T03:06:58.756044Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}