{"doi":"10.1074/jbc.271.39.24207","title":"Structural and Functional Organization of the DNA Polymerase of Bacteriophage T7","abstract":null,"journal":"Journal of Biological Chemistry","year":1996,"id":591807,"datarank":0.703557081448339,"base_score":2.5649493574615367,"endowment":2.5649493574615367,"self_citation_contribution":0.38474240361923057,"citation_network_contribution":0.31881467782910833,"self_endowment_contribution":0.38474240361923057,"citer_contribution":0.31881467782910833,"corpus_percentile":null,"corpus_rank":null,"citation_count":12,"citer_count":7,"citers_with_citation_signal":7,"citers_with_endowment":7,"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":176151,"name":"Charles C. Richardson","orcid":null,"position":1,"is_corresponding":false},{"id":1514275,"name":"Xiao-ming Yang","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Structural and Functional Organization of the DNA Polymerase of Bacteriophage T7","abstract":"The 80-kDa gene 5 protein encoded by bacteriophage T7 shares significant amino acid homology with the large fragment of Escherichia coli DNA polymerase I (Klenow fragment). Like the Klenow fragment, T7 gene 5 protein has both DNA polymerase and 3' to 5' exonuclease activities. However, unlike the Klenow fragment, T7 gene 5 protein binds tightly to E. coli thioredoxin to form a complex that has a high processivity of nucleotide polymerization. In order to identify the domains of gene 5 protein responsible for polymerization, hydrolysis, and binding of thioredoxin, we have analyzed proteolytic fragments of gene 5 protein. Cleavage of the protein within one protease-sensitive region (residue 250-300) yields two molecular weight species of peptides of 32-37 and 43-51 kDa derived from the N-terminal and C-terminal region, respectively. DNA polymerase activity is found within the C-terminal fragments and exonuclease activity within the N-terminal fragments. Thioredoxin stimulates the DNA polymerase activity of the C-terminal fragments. All fragments bind to DNA. In addition to delineating the polymerase and exonuclease domains, the protease-sensitive region appears to interact with E. coli thioredoxin. Thioredoxin protects this region from proteolysis, and alteration of this region reduces the ability of thioredoxin to stimulate polymerase activity.","is_dataset_classified":null,"base_score":2.5649493574615367,"endowment":2.5649493574615367,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"8798663","pmcid":null,"openalex_id":"https://openalex.org/W1968746934","authors":[],"funders":[{"funder_name":"NIAID NIH HHS","grant_id":"AI-06045","title":null}],"total_grants":1,"fwci":2.2537,"citation_percentile":0.85125844,"influential_citations":0,"citation_trend":[],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S0021925818402074/pdf","host_type":"journal"},{"url":"http://www.jbc.org/article/S0021925818402074/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925818402074?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925818402074?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.271.39.24207","host_type":"publisher"},{"url":"https://doi.org/10.1074/jbc.271.39.24207","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/8798663","host_type":"repository"},{"url":"http://nrs.harvard.edu/urn-3:HUL.InstRepos:41483337","host_type":"repository"}],"fields_of_study":["Bacteriophages and microbial interactions","Bacterial Genetics and Biotechnology","RNA and protein synthesis mechanisms"],"mesh_terms":["Amino Acid Sequence","Bacterial Proteins","DNA-Directed DNA Polymerase","Exonucleases","Molecular Sequence Data","Peptide Fragments","Protein Binding","Structure-Activity Relationship","Thioredoxins","Viral Proteins","Sequence Alignment","Sequence Homology, Amino Acid"],"keywords":["Klenow fragment","DNA polymerase I","DNA polymerase II","Molecular biology","DNA polymerase","Biology","DNA clamp","Exonuclease","Polymerase","Processivity","Biochemistry","DNA polymerase mu","DNA","Gene","Circular bacterial chromosome","Reverse transcriptase","Polymerase chain reaction"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-26T10:47:00.129363Z","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":[]}