{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Valentin Gese G"],"funding":["Vetenskapsrådet","Vetenskapsrådet (VR)","Knut och Alice Wallenbergs Stiftelse","Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation)"],"pagination":["6573-6590"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11649783"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["43(24)"],"pubmed_abstract":["Maturation of human mitochondrial tRNA is essential for cellular energy production, yet the underlying mechanisms remain only partially understood. Here, we present several cryo-EM structures of the mitochondrial RNase Z complex (ELAC2/SDR5C1/TRMT10C) bound to different maturation states of mitochondrial tRNA<sup>His</sup>, showing the molecular basis for tRNA-substrate selection and catalysis. Our structural insights provide a molecular rationale for the 5'-to-3' tRNA processing order in mitochondria, the 3'-CCA antideterminant effect, and the basis for sequence-independent recognition of mitochondrial tRNA substrates. Furthermore, our study links mutations in ELAC2 to clinically relevant mitochondrial diseases, offering a deeper understanding of the molecular defects contributing to thes"],"journal":["The EMBO journal"],"pubmed_title":["Structural basis of 3'-tRNA maturation by the human mitochondrial RNase Z complex."],"pmcid":["PMC11649783"],"funding_grant_id":["2017.0080","2022-02326","2018.0080","2018-03808"],"pubmed_authors":["Valentin Gese G","Hallberg BM"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis of 3'-tRNA maturation by the human mitochondrial RNase Z complex.","description":"Maturation of human mitochondrial tRNA is essential for cellular energy production, yet the underlying mechanisms remain only partially understood. Here, we present several cryo-EM structures of the mitochondrial RNase Z complex (ELAC2/SDR5C1/TRMT10C) bound to different maturation states of mitochondrial tRNA<sup>His</sup>, showing the molecular basis for tRNA-substrate selection and catalysis. Our structural insights provide a molecular rationale for the 5'-to-3' tRNA processing order in mitochondria, the 3'-CCA antideterminant effect, and the basis for sequence-independent recognition of mitochondrial tRNA substrates. Furthermore, our study links mutations in ELAC2 to clinically relevant mitochondrial diseases, offering a deeper understanding of the molecular defects contributing to thes","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-06-02T18:04:48.488Z","creation":"2025-04-04T21:45:55.96Z"},"accession":"S-EPMC11649783","cross_references":{"pubmed":["39516281"],"doi":["10.1038/s44318-024-00297-w"]}}