{"doi":"10.1038/s41594-019-0331-x","title":"Mechanism of ribosome stalling during translation of a poly(A) tail","abstract":null,"journal":"Nature Structural & Molecular Biology","year":2019,"id":635888,"datarank":0.7886243058041673,"base_score":5.2574953720277815,"endowment":5.2574953720277815,"self_citation_contribution":0.7886243058041673,"citation_network_contribution":0.0,"self_endowment_contribution":0.7886243058041673,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":191,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":4,"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":277861,"name":"Szymon Juszkiewicz","orcid":"0000-0002-3361-7264","position":1,"is_corresponding":false},{"id":319746,"name":"Junhong Choi","orcid":"0000-0001-9291-5977","position":2,"is_corresponding":false},{"id":319748,"name":"Joseph D. Puglisi","orcid":"0000-0001-9268-5112","position":3,"is_corresponding":false},{"id":631111,"name":"Alan Brown","orcid":"0000-0002-0021-0476","position":4,"is_corresponding":false},{"id":88283,"name":"Sichen Shao","orcid":"0000-0003-2679-5537","position":5,"is_corresponding":false},{"id":236139,"name":"V. Ramakrishnan","orcid":"0000-0002-4699-2194","position":6,"is_corresponding":false},{"id":277865,"name":"Ramanujan S. Hegde","orcid":"0000-0001-8338-852X","position":7,"is_corresponding":false},{"id":1649991,"name":"Viswanathan Chandrasekaran","orcid":"0000-0002-0871-4740","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Mechanism of ribosome stalling during translation of a poly(A) tail","abstract":"Faulty or damaged messenger RNAs are detected by the cell when translating ribosomes stall during elongation and trigger pathways of mRNA decay, nascent protein degradation and ribosome recycling. The most common mRNA defect in eukaryotes is probably inappropriate polyadenylation at near-cognate sites within the coding region. How ribosomes stall selectively when they encounter poly(A) is unclear. Here, we use biochemical and structural approaches in mammalian systems to show that poly-lysine, encoded by poly(A), favors a peptidyl-transfer RNA conformation suboptimal for peptide bond formation. This conformation partially slows elongation, permitting poly(A) mRNA in the ribosome's decoding center to adopt a ribosomal RNA-stabilized single-stranded helix. The reconfigured decoding center clashes with incoming aminoacyl-tRNA, thereby precluding elongation. Thus, coincidence detection of poly-lysine in the exit tunnel and poly(A) in the decoding center allows ribosomes to detect aberrant mRNAs selectively, stall elongation and trigger downstream quality control pathways essential for cellular homeostasis.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":4,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"31768042","pmcid":"PMC6900289","openalex_id":null,"authors":[],"funders":[{"funder_name":"Medical Research Council","grant_id":"1662869","title":null},{"funder_name":"Medical Research Council","grant_id":"MC_U105184332","title":"Structure and function of the translational machinery"},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM051266","title":null},{"funder_name":"Wellcome Trust","grant_id":"096570","title":"Structure and function of ribosomes."},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM113078","title":null},{"funder_name":"Medical Research Council","grant_id":"MC_UP_A022_1007","title":"Membrane protein biosynthesis and quality control"},{"funder_name":"Wellcome Trust","grant_id":"WT096570","title":null},{"funder_name":"National Institutes of Health","grant_id":"5R01GM113078-04","title":"Dynamic pathways of eukaryotic translation initiation"}],"total_grants":8,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"green","license":"Springer TDM","oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6900289","host_type":"repository"},{"url":"http://www.nature.com/articles/s41594-019-0331-x.pdf","host_type":"publisher"},{"url":"http://www.nature.com/articles/s41594-019-0331-x","host_type":"publisher"},{"url":"https://europepmc.org/articles/PMC6900289","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC6900289?pdf=render","host_type":"Europe_PMC"},{"url":"https://doi.org/10.1038/s41594-019-0331-x","host_type":""},{"url":"https://europepmc.org/articles/pmc6900289?pdf=render","host_type":""},{"url":"https://pubmed.ncbi.nlm.nih.gov/31768042","host_type":""},{"url":"http://dx.doi.org/10.1038/s41594-019-0331-x","host_type":""},{"url":"https://dx.doi.org/10.1038/s41594-019-0331-x","host_type":""}],"fields_of_study":["0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":["Ribosomes","Humans","Polylysine","RNA, Transfer, Amino Acyl","Peptides","RNA, Messenger","RNA, Transfer","Poly A","Protein Biosynthesis","Polyadenylation","Nucleic Acid Conformation","RNA Stability","Models, Molecular","HEK293 Cells"],"keywords":["Models, Molecular","RNA Stability","RNA, Transfer, Amino Acyl","Polyadenylation","Article","HEK293 Cells","RNA, Transfer","Protein Biosynthesis","Humans","Nucleic Acid Conformation","Polylysine","RNA, Messenger","Peptides","Poly A","Ribosomes"],"sdg_mappings":[],"linked_datasets":[{"doi":"10.6084/m9.figshare.13524909.v1","title":"Additional file 1 of Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.13524909","title":"Additional file 1 of Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.13524912.v1","title":"Additional file 2 of Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.13524912","title":"Additional file 2 of Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding","publisher":"figshare","resource_type":"JournalArticle"}],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"},{"name":"doi"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-06T15:45:58.954529Z","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":[]}