{"doi":"10.1093/jb/mvz006","title":"Domains two and three of <i>Escherichia coli</i> ribosomal S1 protein confers 30S subunits a high affinity for downstream A/U-rich mRNAs","abstract":null,"journal":"The Journal of Biochemistry","year":2019,"id":67966,"datarank":0.5806545487676084,"base_score":2.1972245773362196,"endowment":2.1972245773362196,"self_citation_contribution":0.32958368660043297,"citation_network_contribution":0.2510708621671754,"self_endowment_contribution":0.32958368660043297,"citer_contribution":0.2510708621671754,"corpus_percentile":null,"corpus_rank":null,"citation_count":8,"citer_count":8,"citers_with_citation_signal":8,"citers_with_endowment":8,"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":360500,"name":"Lizbeth Hernández-Ancheyta","orcid":null,"position":1,"is_corresponding":false},{"id":360501,"name":"Gabriel Guarneros","orcid":null,"position":2,"is_corresponding":false},{"id":360502,"name":"N Oviedo","orcid":null,"position":3,"is_corresponding":false},{"id":360503,"name":"Javier Hernández-Sánchez","orcid":null,"position":4,"is_corresponding":false},{"id":360499,"name":"Juan C Cifuentes-Goches","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Domains two and three of <i>Escherichia coli</i> ribosomal S1 protein confers 30S subunits a high affinity for downstream A/U-rich mRNAs","abstract":"S1, a multi-domain ribosomal protein associated with the 30S subunit, is essential for translation initiation. S1 binds with high affinity to single-stranded mRNA containing A/U-rich patches upstream of the start codon. It was previously reported that domains 1-3 of S1 protein play a role in the docking and unfolding of structured mRNAs to the ribosome. Moreover, S1-deficient 30S subunits are still able to bind to low structured mRNAs. However, mRNAs containing A/U-rich patches in the early base positions after start codon enhance protein synthesis and mRNA binding to the ribosome, which suggests that S1 is also able to interact with these A/U-rich regions. To evaluate the essentiality of S1 domains in the binding to low structured mRNAs containing A/U/G nucleotides after the start codon as well as their role in translation and cell viability, S1 protein deletion variants were generated. We show that S1 domain 3 is necessary to discriminate these mRNAs according to the nucleotide nature since its absence abrogated S1 binding to A/U-rich mRNAs and allowed binding to G-rich mRNAs. Interestingly, domains 2 and 3 were required for the binding of mRNAs containing A/U-rich sequences after the start codon to 30S, in vitro translation and cell viability.","is_dataset_classified":null,"base_score":2.1972245773362196,"endowment":2.1972245773362196,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"30668774","pmcid":null,"openalex_id":"https://openalex.org/W2912635769","authors":[],"funders":[{"funder_name":"CONACyT México","grant_id":"27975","title":null}],"total_grants":1,"fwci":0.4143,"citation_percentile":0.59917881,"influential_citations":0,"citation_trend":[{"year":2020,"count":3},{"year":2021,"count":2},{"year":2023,"count":3}],"oa_status":"closed","license":"https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model","oa_locations":[{"url":"http://academic.oup.com/jb/advance-article-pdf/doi/10.1093/jb/mvz006/27714693/mvz006.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1093/jb/mvz006","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/30668774","host_type":"repository"}],"fields_of_study":["RNA and protein synthesis mechanisms","RNA modifications and cancer","Viral Infections and Immunology Research","Chemistry","Medicine","Biology","Animals","Escherichia coli","Female","Protein Domains","RNA, Messenger","Rats","Rats, Wistar","Ribosomal Proteins","Ribosome Subunits, Small, Bacterial"],"mesh_terms":["Protein Domains","Animals","Escherichia coli","Female","Ribosomal Proteins","RNA, Messenger","Rats, Wistar","Rats","Ribosome Subunits, Small, Bacterial"],"keywords":["Start codon","30S","Ribosomal binding site","Ribosome","Shine-Dalgarno sequence","Biology","Messenger RNA","Ribosomal protein","Translation (biology)","Molecular biology","Eukaryotic translation","Eukaryotic Ribosome","Cell biology","Genetics","RNA","Gene","Ribosomal Protein S1","A/u/g-rich Mrnas","S1 Domains"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Reduced inequalities"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-18T21:22:10.859755Z","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":[]}