{"doi":"10.1073/pnas.94.2.479","title":"The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on\n            <i>Escherichia coli</i>\n            DNA polymerase I","abstract":"<jats:p>\n            Bacteriophage T7 DNA polymerase shares extensive sequence homology with\n            <jats:italic>Escherichia coli</jats:italic>\n            DNA polymerase I. However,\n            <jats:italic>in vivo</jats:italic>\n            ,\n            <jats:italic>E. coli</jats:italic>\n            DNA polymerase I is involved primarily in the repair of DNA whereas T7 DNA polymerase is responsible for the replication of the viral genome. In accord with these roles, T7 DNA polymerase is highly processive while\n            <jats:italic>E. coli</jats:italic>\n            DNA polymerase I has low processivity. The high processivity of T7 DNA polymerase is achieved through tight binding to its processivity factor,\n            <jats:italic>E. coli</jats:italic>\n            thioredoxin. We have identified a unique 76-residue domain in T7 DNA polymerase responsible for this interaction. Insertion of this domain into the homologous site in\n            <jats:italic>E. coli</jats:italic>\n            DNA polymerase I results in a dramatic increase in the processivity of the chimeric DNA polymerase, a phenomenon that is dependent upon its binding to thioredoxin.\n          </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1997,"id":33377,"datarank":3.7317679939381874,"base_score":4.574710978503383,"endowment":4.574710978503383,"self_citation_contribution":0.6862066467755076,"citation_network_contribution":3.0455613471626797,"self_endowment_contribution":0.6862066467755076,"citer_contribution":3.0455613471626797,"corpus_percentile":null,"corpus_rank":null,"citation_count":96,"citer_count":76,"citers_with_citation_signal":60,"citers_with_endowment":60,"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":174794,"name":"Stanley Tabor","orcid":null,"position":1,"is_corresponding":false},{"id":174797,"name":"Charles C. Richardson","orcid":null,"position":2,"is_corresponding":false},{"id":174792,"name":"Ella Bedford","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":4.574710978503383,"endowment":4.574710978503383,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"9012809","pmcid":"PMC19538","openalex_id":"https://openalex.org/W2014976263","authors":[],"funders":[{"funder_name":"NIAID NIH HHS","grant_id":"AI-06045","title":null}],"total_grants":1,"fwci":5.5945,"citation_percentile":0.96163031,"influential_citations":2,"citation_trend":[{"year":2012,"count":3},{"year":2013,"count":3},{"year":2015,"count":3},{"year":2017,"count":3},{"year":2018,"count":3},{"year":2019,"count":3},{"year":2020,"count":3},{"year":2021,"count":6},{"year":2022,"count":4},{"year":2023,"count":4},{"year":2024,"count":3},{"year":2025,"count":3},{"year":2026,"count":3}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://www.pnas.org/doi/pdf/10.1073/pnas.94.2.479","host_type":"journal"},{"url":"https://www.pnas.org/doi/pdf/10.1073/pnas.94.2.479","host_type":"BRONZE"},{"url":"https://www.pnas.org/doi/pdf/10.1073/pnas.94.2.479","host_type":"publisher"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.94.2.479","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.94.2.479","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/9012809","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/19538","host_type":"repository"}],"fields_of_study":["Bacteriophages and microbial interactions","Bacterial Genetics and Biotechnology","RNA and protein synthesis mechanisms","Biology","Medicine","Chemistry","Bacteriophage T7","Binding Sites","Chemical Phenomena","Chemistry, Physical","DNA","DNA Polymerase I","DNA-Directed DNA Polymerase","Escherichia coli","Protein Binding","Recombinant Fusion Proteins","Structure-Activity Relationship","Surface Properties","Thioredoxins"],"mesh_terms":["Binding Sites","Chemistry, Physical","DNA","DNA Polymerase I","DNA-Directed DNA Polymerase","Escherichia coli","Protein Binding","Recombinant Fusion Proteins","Structure-Activity Relationship","Surface Properties","Thioredoxins","Bacteriophage T7","Chemical Phenomena"],"keywords":["Processivity","DNA polymerase II","DNA polymerase","DNA polymerase I","DNA clamp","Polymerase","Biology","Molecular biology","DNA polymerase delta","DNA","Biochemistry","Gene","Polymerase chain reaction","Reverse transcriptase"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-09T16:09:12.931580Z","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":[]}