9HCF

Mouse mitoribosome large subunit assembly intermediate bound to NSUN4, METRF4, GTPBP7, GTPBP10 and the MALSU-L0R8F8-mtACP complex with uL16m, State B2 (SAMC knock-out)

これはPDB形式変換不可エントリーです。

9HCF の概要

• エントリーDOI: 10.2210/pdb9hcf/pdb
• 関連するPDBエントリー: 9E9C 9HCC 9HCD 9HCE 9HCG 9HCH
• EMDBエントリー: 52047
• 分子名称: 16S rRNA (1432-MER), Large ribosomal subunit protein uL14m, Large ribosomal subunit protein uL15m, ... (63 entities in total)
• 機能のキーワード: mitochondria, ribosome assembly, large subunit, ribosome
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 59
• 化学式量合計: 1954314.21

構造登録者

Singh, V.,Rorbach, J.,Freyer, C.,Amunts, A.,Wredenberg, A. (登録日: 2024-11-08, 公開日: 2025-07-09, 最終更新日: 2025-07-16)

主引用文献

Glasgow, R.I.C.,Singh, V.,Pena-Perez, L.,Wilhalm, A.,Moedas, M.F.,Moore, D.,Rosenberger, F.A.,Li, X.,Atanassov, I.,Saba, M.,Cipullo, M.,Rorbach, J.,Wedell, A.,Freyer, C.,Amunts, A.,Wredenberg, A.
The mitochondrial methylation potential gates mitoribosome assembly.
Nat Commun, 16:5388-5388, 2025

PubMed Abstract: S-adenosylmethionine (SAM) is the principal methyl donor in cells and is essential for mitochondrial gene expression, influencing RNA modifications, translation, and ribosome biogenesis. Using direct long-read RNA sequencing in mouse tissues and embryonic fibroblasts, we show that processing of the mitochondrial ribosomal gene cluster fails in the absence of mitochondrial SAM, leading to an accumulation of unprocessed precursors. Proteomic analysis of ribosome fractions revealed these precursors associated with processing and assembly factors, indicating stalled biogenesis. Structural analysis by cryo-electron microscopy demonstrated that SAM-dependent methylation is required for peptidyl transferase centre formation during mitoribosome assembly. Our findings identify a critical role for SAM in coordinating mitoribosomal RNA processing and large subunit maturation, linking cellular methylation potential to mitochondrial translation capacity.

PubMed: 40562754
DOI: 10.1038/s41467-025-60977-x

実験手法

ELECTRON MICROSCOPY (2.85 Å)