{"doi":"10.1101/gad.328443.119","title":"Beyond rRNA and snRNA: tRNA as a 2′-O-methylation target for nucleolar and Cajal body box C/D RNPs","abstract":"<jats:p>Box C/D small nucleolar RNAs (snoRNAs) and small Cajal body (CB) RNAs (scaRNAs) form ribonucleoprotein (RNP) complexes to mediate 2′-O-methylation of rRNAs and small nuclear RNAs (snRNAs), respectively. The site of methylation is determined by antisense elements in the box C/D RNAs that are complementary to sequences in target RNAs. However, numerous box C/D RNAs in mammalian cells lack antisense elements to rRNAs or snRNAs; thus, their targets remain unknown. In this issue of <jats:italic>Genes &amp; Development</jats:italic>, Vitali and Kiss (pp. 741–746) demonstrate that “orphan” nucleolar box C/D snoRNA SNORD97 and CB box C/D scaRNA SCARNA97 contain antisense elements that target the wobble cytidine at position 34 of human elongator tRNA<jats:sup>Met</jats:sup>(CAT) for 2′-O-methylation (C<jats:sub>34</jats:sub>m). C<jats:sub>34</jats:sub>m is jointly mediated by SNORD97 and SCARNA97 despite their apparently different intranuclear locations. Furthermore, the investigators demonstrate that C<jats:sub>34</jats:sub>m prohibits site-specific cleavage of tRNA<jats:sup>Met</jats:sup> (CAT) into tRNA fragments (tRFs) by the stress-responsive endoribonuclease angiogenin, thereby uncovering a role for SNORD97 and SCARNA97 in the biogenesis of tRFs, which modulate a diverse set of cellular functions in human health and disease.</jats:p>","journal":"Genes &amp; Development","year":2019,"id":592951,"datarank":1.0354798079116154,"base_score":3.4657359027997265,"endowment":3.4657359027997265,"self_citation_contribution":0.519860385419959,"citation_network_contribution":0.5156194224916565,"self_endowment_contribution":0.519860385419959,"citer_contribution":0.5156194224916565,"corpus_percentile":null,"corpus_rank":null,"citation_count":31,"citer_count":25,"citers_with_citation_signal":17,"citers_with_endowment":17,"datacite_reuse_total":6,"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":367378,"name":"Anita K. Hopper","orcid":"0000-0002-7884-2932","position":1,"is_corresponding":false},{"id":1517438,"name":"Regina T. Nostramo","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Beyond rRNA and snRNA: tRNA as a 2′-O-methylation target for nucleolar and Cajal body box C/D RNPs","abstract":"<jats:p>Box C/D small nucleolar RNAs (snoRNAs) and small Cajal body (CB) RNAs (scaRNAs) form ribonucleoprotein (RNP) complexes to mediate 2′-O-methylation of rRNAs and small nuclear RNAs (snRNAs), respectively. The site of methylation is determined by antisense elements in the box C/D RNAs that are complementary to sequences in target RNAs. However, numerous box C/D RNAs in mammalian cells lack antisense elements to rRNAs or snRNAs; thus, their targets remain unknown. In this issue of <jats:italic>Genes &amp; Development</jats:italic>, Vitali and Kiss (pp. 741–746) demonstrate that “orphan” nucleolar box C/D snoRNA SNORD97 and CB box C/D scaRNA SCARNA97 contain antisense elements that target the wobble cytidine at position 34 of human elongator tRNA<jats:sup>Met</jats:sup>(CAT) for 2′-O-methylation (C<jats:sub>34</jats:sub>m). C<jats:sub>34</jats:sub>m is jointly mediated by SNORD97 and SCARNA97 despite their apparently different intranuclear locations. Furthermore, the investigators demonstrate that C<jats:sub>34</jats:sub>m prohibits site-specific cleavage of tRNA<jats:sup>Met</jats:sup> (CAT) into tRNA fragments (tRFs) by the stress-responsive endoribonuclease angiogenin, thereby uncovering a role for SNORD97 and SCARNA97 in the biogenesis of tRFs, which modulate a diverse set of cellular functions in human health and disease.</jats:p>","is_dataset_classified":null,"base_score":3.4657359027997265,"endowment":3.4657359027997265,"datacite_reuse_total":6,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"31262844","pmcid":"PMC6601515","openalex_id":"https://openalex.org/W2953671244","authors":[],"funders":[{"funder_name":"National Institutes of Health","grant_id":"GM122884","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM122884","title":null},{"funder_name":"National Institutes of Health","grant_id":"5R01GM122884-06","title":"tRNA processing and nuclear-cytoplasmic dynamics"}],"total_grants":3,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[{"year":2020,"count":4},{"year":2021,"count":1},{"year":2022,"count":8},{"year":2023,"count":10},{"year":2024,"count":2},{"year":2025,"count":3},{"year":2026,"count":3}],"oa_status":"gold","license":"cc-by-nc","oa_locations":[{"url":"http://genesdev.cshlp.org/content/33/13-14/739.full.pdf","host_type":"journal"},{"url":"http://genesdev.cshlp.org/content/33/13-14/739.full.pdf","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1101/gad.328443.119","host_type":"publisher"},{"url":"https://doi.org/10.1101/gad.328443.119","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/31262844","host_type":"repository"},{"url":"http://genesdev.cshlp.org/cgi/content/short/33/13-14/739","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6601515","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC6601515","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC6601515?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1101/gad.328443.119","host_type":""},{"url":"https://dx.doi.org/10.1101/gad.328443.119","host_type":""}],"fields_of_study":["RNA modifications and cancer","Cancer-related molecular mechanisms research","RNA Research and Splicing","0301 basic medicine","03 medical and health sciences"],"mesh_terms":["Animals","Cytidine","Humans","Methylation","Ribonucleoproteins","RNA, Transfer, Met","RNA, Small Nucleolar","Coiled Bodies"],"keywords":["Small nucleolar RNA","Biology","Cajal body","Small nuclear RNA","Ribonucleoprotein","Transfer RNA","snRNP","Methylation","RNA","Small nuclear ribonucleoprotein","Guide RNA","Nucleolus","Polyadenylation","Cell biology","Genetics","Non-coding RNA","RNA splicing","Gene","Genome","Angiogenin","2′-O-methylation","Trna-derived Fragment","Small Cajal Body Rna","Box C/d Small Nucleolar Rna","RNA, Transfer, Met","Ribonucleoproteins","Animals","Humans","RNA, Small Nucleolar","Coiled Bodies","Cytidine","Outlook"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. Good health"}],"linked_datasets":[{"doi":"10.6084/m9.figshare.22615661.v1","title":"Additional file 1 of C/D box small nucleolar RNA SNORD104 promotes endometrial cancer by regulating the 2ʹ-O-methylation of PARP1","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.22615661","title":"Additional file 1 of C/D box small nucleolar RNA SNORD104 promotes endometrial cancer by regulating the 2ʹ-O-methylation of PARP1","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.22615667.v1","title":"Additional file 3 of C/D box small nucleolar RNA SNORD104 promotes endometrial cancer by regulating the 2ʹ-O-methylation of PARP1","publisher":"figshare","resource_type":"Image"},{"doi":"10.6084/m9.figshare.22615664","title":"Additional file 2 of C/D box small nucleolar RNA SNORD104 promotes endometrial cancer by regulating the 2ʹ-O-methylation of PARP1","publisher":"figshare","resource_type":"Image"},{"doi":"10.6084/m9.figshare.22615667","title":"Additional file 3 of C/D box small nucleolar RNA SNORD104 promotes endometrial cancer by regulating the 2ʹ-O-methylation of PARP1","publisher":"figshare","resource_type":"Image"},{"doi":"10.6084/m9.figshare.22615664.v1","title":"Additional file 2 of C/D box small nucleolar RNA SNORD104 promotes endometrial cancer by regulating the 2ʹ-O-methylation of PARP1","publisher":"figshare","resource_type":"Image"}],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-26T16:21:21.429626Z","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":[]}