8RR3

Human mitochondrial RNase Z complex with ELAC2-D550N catalytic mutant and tRNA-Gln precursor (Composite model)

8RR3 の概要

• エントリーDOI: 10.2210/pdb8rr3/pdb
• EMDBエントリー: 19455
• 分子名称: 3-hydroxyacyl-CoA dehydrogenase type-2, Zinc phosphodiesterase ELAC protein 2, tRNA methyltransferase 10 homolog C, ... (6 entities in total)
• 機能のキーワード: trna processing, rnase z, endonuclease, mitochondrial, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 265696.03

構造登録者

Bhatta, A.,Yu, R.D.,Kuhle, B.,Hillen, H.S. (登録日: 2024-01-22, 公開日: 2025-01-08, 最終更新日: 2025-12-10)

主引用文献

Bhatta, A.,Kuhle, B.,Yu, R.D.,Spanaus, L.,Ditter, K.,Bohnsack, K.E.,Hillen, H.S.
Molecular basis of human nuclear and mitochondrial tRNA 3' processing.
Nat.Struct.Mol.Biol., 32:613-624, 2025

PubMed Abstract: Eukaryotic transfer RNA (tRNA) precursors undergo sequential processing steps to become mature tRNAs. In humans, ELAC2 carries out 3' end processing of both nucleus-encoded (nu-tRNAs) and mitochondria-encoded (mt-tRNAs) tRNAs. ELAC2 is self-sufficient for processing of nu-tRNAs but requires TRMT10C and SDR5C1 to process most mt-tRNAs. Here we show that TRMT10C and SDR5C1 specifically facilitate processing of structurally degenerate mt-tRNAs lacking the canonical elbow. Structures of ELAC2 in complex with TRMT10C, SDR5C1 and two divergent mt-tRNA substrates reveal two distinct mechanisms of pre-tRNA recognition. While canonical nu-tRNAs and mt-tRNAs are recognized by direct ELAC2-RNA interactions, processing of noncanonical mt-tRNAs depends on protein-protein interactions between ELAC2 and TRMT10C. These results provide the molecular basis for tRNA 3' processing in both the nucleus and the mitochondria and explain the organelle-specific requirement for additional factors. Moreover, they suggest that TRMT10C-SDR5C1 evolved as a mitochondrial tRNA maturation platform to compensate for the structural erosion of mt-tRNAs in bilaterian animals.

PubMed: 39747487
DOI: 10.1038/s41594-024-01445-w

実験手法

ELECTRON MICROSCOPY (3.4 Å)