{"doi":"10.1101/gad.7.5.870","title":"Oxytricha telomere-binding protein: separable DNA-binding and dimerization domains of the alpha-subunit.","abstract":"<jats:p>A telomere-binding protein heterodimer of 56-kD (alpha) and 41-kD (beta) subunits binds to the single-stranded (T4G4)2 terminus of each Oxytricha nova macronuclear DNA molecule. The alpha-subunit by itself binds to telomeric DNA. The beta-subunit alone does not bind to DNA specifically but interacts with the alpha-subunit to form a very stable ternary complex. We show that the formation of alpha-beta-DNA ternary complex is extremely cooperative. Furthermore, the binary complex (alpha-DNA) has a dissociation half-life of much less than 1 min; addition of the beta-subunit increases the half-life to approximately 100 hrs. Libraries of plasmids with random deletions of the open reading frame for the alpha-subunit were introduced into Escherichia coli, and extracts were subsequently checked for both protein expression and DNA-binding activity with or without added beta-subunit. The alpha-subunit was found to contain two structurally separable domains with distinct functions. The amino-terminal two-thirds is necessary and sufficient for sequence-specific DNA binding. The carboxy-terminal one-third is responsible for alpha/beta-subunit interactions. When expressed separately in E. coli, purified, and mixed together, these two domains reconstitute the activity of the wild-type alpha-subunit (trans-complementation in vitro). The amino-terminal two-thirds of the beta-subunit is necessary and sufficient both for alpha/beta-subunit interactions and for ternary complex formation. We conclude that the alpha-subunit of the telomere-binding protein, like many transcription factors, has separable DNA-binding and protein-protein interaction domains.</jats:p>","journal":"Genes &amp; Development","year":1993,"id":24616,"datarank":3.7956632340802705,"base_score":4.204692619390966,"endowment":4.204692619390966,"self_citation_contribution":0.6307038929086449,"citation_network_contribution":3.1649593411716257,"self_endowment_contribution":0.6307038929086449,"citer_contribution":3.1649593411716257,"corpus_percentile":null,"corpus_rank":null,"citation_count":66,"citer_count":54,"citers_with_citation_signal":53,"citers_with_endowment":53,"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":147215,"name":"J T Gray","orcid":null,"position":1,"is_corresponding":false},{"id":147216,"name":"T R Cech","orcid":null,"position":2,"is_corresponding":false},{"id":147214,"name":"G Fang","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":4.204692619390966,"endowment":4.204692619390966,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"8491383","pmcid":null,"openalex_id":"https://openalex.org/W2023377008","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM28039","title":null}],"total_grants":1,"fwci":null,"citation_percentile":null,"influential_citations":6,"citation_trend":[{"year":2013,"count":1},{"year":2017,"count":1}],"oa_status":"gold","license":null,"oa_locations":[{"url":"http://genesdev.cshlp.org/content/7/5/870.full.pdf","host_type":"journal"},{"url":"https://doi.org/10.1101/gad.7.5.870","host_type":"GOLD"},{"url":"http://genesdev.cshlp.org/content/7/5/870.full.pdf","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1101/gad.7.5.870","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/8491383","host_type":"repository"}],"fields_of_study":["Telomeres, Telomerase, and Senescence","CRISPR and Genetic Engineering","Advanced biosensing and bioanalysis techniques","Biology","Medicine","Chemistry","Animals","Base Sequence","DNA Probes","DNA, Protozoan","DNA-Binding Proteins","Electrophoresis, Polyacrylamide Gel","Escherichia coli","Gene Expression Regulation","Gene Library","Molecular Sequence Data","Mutagenesis, Site-Directed","Oligonucleotide Probes","Oxytricha","Plasmids","Protozoan Proteins","Recombinant Proteins","Sequence Homology, Nucleic Acid","Time Factors","Transcription, Genetic"],"mesh_terms":["Animals","Base Sequence","DNA-Binding Proteins","Electrophoresis, Polyacrylamide Gel","Escherichia coli","Gene Expression Regulation","Molecular Sequence Data","Plasmids","Recombinant Proteins","Sequence Homology, Nucleic Acid","Time Factors","Transcription, Genetic","DNA Probes","Oligonucleotide Probes","Gene Library","Protozoan Proteins","DNA, Protozoan","Mutagenesis, Site-Directed","Oxytricha"],"keywords":["Biology","Interleukin 10 receptor, alpha subunit","Protein subunit","Gamma-aminobutyric acid receptor subunit alpha-1","Specificity factor","Interleukin 5 receptor alpha subunit","Molecular biology","SCN3A","G alpha subunit","Gi alpha subunit","DNA","Biochemistry","Gene"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-07T22:51:08.926871Z","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":[]}