{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hu Y"],"funding":["Welch Foundation (The Welch Foundation)","NICHD NIH HHS","Cancer Prevention and Research Institute of Texas (CPRIT)","Foundation for the NIH","NCI NIH HHS","Welch Foundation","Foundation for the NIH (FNIH)","HHMI","NIGMS NIH HHS","HHMI (HHMI)","Cancer Prevention and Research Institute of Texas"],"pagination":["e2408249121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11494293"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(42)"],"pubmed_abstract":["ATP-grasp superfamily enzymes contain a hand-like ATP-binding fold and catalyze a variety of reactions using a similar catalytic mechanism. More than 30 protein families are categorized in this superfamily, and they are involved in a plethora of cellular processes and human diseases. Here, we identify C12orf29 (RLIG1) as an atypical ATP-grasp enzyme that ligates RNA. Human RLIG1 and its homologs autoadenylate on an active site Lys residue as part of a reaction intermediate that specifically ligates RNA halves containing a 5'-phosphate and a 3'-hydroxyl. RLIG1 binds tRNA in cells and can ligate tRNA within the anticodon loop in vitro. Transcriptomic analyses of <i>Rlig1</i> knockout mice revealed significant alterations in global tRNA levels in the brains of female mice, but not in those of"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation."],"pmcid":["PMC11494293"],"funding_grant_id":["N/A","I-2088","DP2 GM137419","R35 GM136216","I-1961","R01 HD103627","I-1911","R01 CA282036","RP220309","DP2GM137419","R01CA282036","RR150033","Hanna Gray fellowship"],"pubmed_authors":["Wu J","Tagliabracci VS","Hu Y","Lambowitz AM","Song B","Tomchick DR","Pawlowski K","Xu H","Pfister JP","Mendell JT","Wang T","Sakurai M","Jones BT","Servage KA","Lopez VA"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation.","description":"ATP-grasp superfamily enzymes contain a hand-like ATP-binding fold and catalyze a variety of reactions using a similar catalytic mechanism. More than 30 protein families are categorized in this superfamily, and they are involved in a plethora of cellular processes and human diseases. Here, we identify C12orf29 (RLIG1) as an atypical ATP-grasp enzyme that ligates RNA. Human RLIG1 and its homologs autoadenylate on an active site Lys residue as part of a reaction intermediate that specifically ligates RNA halves containing a 5'-phosphate and a 3'-hydroxyl. RLIG1 binds tRNA in cells and can ligate tRNA within the anticodon loop in vitro. Transcriptomic analyses of <i>Rlig1</i> knockout mice revealed significant alterations in global tRNA levels in the brains of female mice, but not in those of","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-07-15T04:05:49.973Z","creation":"2025-04-04T00:29:33.238Z"},"accession":"S-EPMC11494293","cross_references":{"pubmed":["39388274"],"doi":["10.1073/pnas.2408249121"]}}