{"doi":"10.1261/rna.971208","title":"Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking","abstract":"<jats:p>Cap-dependent ribosome recruitment to eukaryotic mRNAs during translation initiation is stimulated by the eukaryotic initiation factor (eIF) 4F complex and eIF4B. eIF4F is a heterotrimeric complex composed of three subunits: eIF4E, a 7-methyl guanosine cap binding protein; eIF4A, a DEAD-box RNA helicase; and eIF4G. The interactions of eIF4E, eIF4A, and eIF4B with mRNA have previously been monitored by chemical- and UV-based cross-linking approaches aimed at characterizing the initial protein/mRNA interactions that lead to ribosome recruitment. These studies have led to a model whereby eIF4E interacts with the 7-methyl guanosine cap structure in an ATP-independent manner, followed by an ATP-dependent interaction of eIF4A and eIF4B. Herein, we apply a splint-ligation-mediated approach to generate 4-thiouridine-containing mRNA adjacent to a radiolabel group that we utilize to monitor cap-dependent cross-linking of proteins adjacent to, and downstream from, the cap structure. Using this approach, we demonstrate interactions between eIF4G, eIF4H, and eIF3 subunits with the mRNA during the cap recognition process.</jats:p>","journal":"RNA","year":2008,"id":22261,"datarank":2.2451194357013162,"base_score":3.9889840465642745,"endowment":3.9889840465642745,"self_citation_contribution":0.5983476069846413,"citation_network_contribution":1.646771828716675,"self_endowment_contribution":0.5983476069846413,"citer_contribution":1.646771828716675,"corpus_percentile":null,"corpus_rank":null,"citation_count":53,"citer_count":44,"citers_with_citation_signal":37,"citers_with_endowment":37,"datacite_reuse_total":2,"is_dataset":false,"is_dataset_confidence":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":117476,"name":"Hiroaki Imataka","orcid":null,"position":1,"is_corresponding":false},{"id":137186,"name":"Jerry Pelletier","orcid":null,"position":2,"is_corresponding":false},{"id":140555,"name":"Lisa Lindqvist","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":3.9889840465642745,"endowment":3.9889840465642745,"datacite_reuse_total":2,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"18367715","pmcid":"PMC2327359","openalex_id":"https://openalex.org/W2148144810","authors":[],"funders":[],"total_grants":0,"fwci":1.544,"citation_percentile":0.82515768,"influential_citations":2,"citation_trend":[{"year":2012,"count":6},{"year":2013,"count":3},{"year":2014,"count":3},{"year":2015,"count":1},{"year":2016,"count":5},{"year":2017,"count":5},{"year":2018,"count":2},{"year":2019,"count":2},{"year":2021,"count":1},{"year":2022,"count":7},{"year":2023,"count":4},{"year":2024,"count":2},{"year":2025,"count":1},{"year":2026,"count":2}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"http://rnajournal.cshlp.org/content/14/5/960.full.pdf","host_type":"journal"},{"url":"http://rnajournal.cshlp.org/content/14/5/960.full.pdf","host_type":"BRONZE"},{"url":"http://rnajournal.cshlp.org/content/14/5/960.full.pdf","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1261/rna.971208","host_type":"publisher"},{"url":"https://doi.org/10.1261/rna.971208","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/18367715","host_type":"repository"},{"url":"http://rnajournal.cshlp.org/cgi/content/short/14/5/960","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2327359","host_type":"repository"}],"fields_of_study":["RNA and protein synthesis mechanisms","RNA Research and Splicing","RNA modifications and cancer","Biology","Medicine","Chemistry","Adenosine Triphosphate","Animals","Base Sequence","Cross-Linking Reagents","Eukaryotic Initiation Factor-3","Eukaryotic Initiation Factor-4G","Eukaryotic Initiation Factors","In Vitro Techniques","Mice","Models, Biological","Molecular Sequence Data","Peptide Chain Initiation, Translational","Peptide Initiation Factors","RNA Caps","RNA, Messenger","Recombinant Proteins","Ultraviolet Rays"],"mesh_terms":["Adenosine Triphosphate","Animals","Base Sequence","Cross-Linking Reagents","Models, Biological","Molecular Sequence Data","Peptide Chain Initiation, Translational","Peptide Initiation Factors","Recombinant Proteins","RNA Caps","RNA, Messenger","Ultraviolet Rays","Eukaryotic Initiation Factor-4G","Eukaryotic Initiation Factor-3","Eukaryotic Initiation Factors","Mice","In Vitro Techniques"],"keywords":["EIF4G","EIF4E","eIF4A","Initiation factor","Eukaryotic initiation factor","Biology","Messenger RNA","Eukaryotic translation","EIF4A1","Cell biology","RNA Helicase A","Guanosine","eIF2","Translation (biology)","Biochemistry","RNA","Helicase","Gene"],"sdg_mappings":[],"linked_datasets":[{"doi":"10.6084/m9.figshare.20921226.v1","title":"Additional file 1 of Novel eIF4A1 inhibitors with anti‐tumor activity in lymphoma","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.20921226","title":"Additional file 1 of Novel eIF4A1 inhibitors with anti‐tumor activity in lymphoma","publisher":"figshare","resource_type":"JournalArticle"}],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-06T18:28:21.664867Z","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":[]}