7ONU

Structure of human mitochondrial RNase P in complex with mitochondrial pre-tRNA-Tyr

7ONU の概要

• エントリーDOI: 10.2210/pdb7onu/pdb
• EMDBエントリー: 13002
• 分子名称: 3-hydroxyacyl-CoA dehydrogenase type-2, Mitochondrial ribonuclease P catalytic subunit, tRNA methyltransferase 10 homolog C, ... (7 entities in total)
• 機能のキーワード: rna processing, mitochondria, gene expression, transcription, translation, 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: 257422.96

構造登録者

Bhatta, A.,Dienemann, C.,Cramer, P.,Hillen, H.S. (登録日: 2021-05-26, 公開日: 2021-08-11, 最終更新日: 2024-07-10)

主引用文献

Bhatta, A.,Dienemann, C.,Cramer, P.,Hillen, H.S.
Structural basis of RNA processing by human mitochondrial RNase P.
Nat.Struct.Mol.Biol., 28:713-723, 2021

PubMed Abstract: Human mitochondrial transcripts contain messenger and ribosomal RNAs flanked by transfer RNAs (tRNAs), which are excised by mitochondrial RNase (mtRNase) P and Z to liberate all RNA species. In contrast to nuclear or bacterial RNase P, mtRNase P is not a ribozyme but comprises three protein subunits that carry out RNA cleavage and methylation by unknown mechanisms. Here, we present the cryo-EM structure of human mtRNase P bound to precursor tRNA, which reveals a unique mechanism of substrate recognition and processing. Subunits TRMT10C and SDR5C1 form a subcomplex that binds conserved mitochondrial tRNA elements, including the anticodon loop, and positions the tRNA for methylation. The endonuclease PRORP is recruited and activated through interactions with its PPR and nuclease domains to ensure precise pre-tRNA cleavage. The structure provides the molecular basis for the first step of RNA processing in human mitochondria.

PubMed: 34489609
DOI: 10.1038/s41594-021-00637-y

実験手法

ELECTRON MICROSCOPY (3 Å)