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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)

This is a non-PDB format compatible entry.
Summary for 9HCF
Entry DOI10.2210/pdb9hcf/pdb
Related9E9C 9HCC 9HCD 9HCE 9HCG 9HCH
EMDB information52047
Descriptor16S rRNA (1432-MER), Large ribosomal subunit protein uL14m, Large ribosomal subunit protein uL15m, ... (63 entities in total)
Functional Keywordsmitochondria, ribosome assembly, large subunit, ribosome
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains59
Total formula weight1954314.21
Authors
Singh, V.,Rorbach, J.,Freyer, C.,Amunts, A.,Wredenberg, A. (deposition date: 2024-11-08, release date: 2025-07-09, Last modification date: 2025-07-16)
Primary citationGlasgow, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.85 Å)
Structure validation

238895

数据于2025-07-16公开中

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