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9HFO

Translation-initiation state of human mitochondrial ribosome small subunit (State G)

Summary for 9HFO
Entry DOI10.2210/pdb9hfo/pdb
EMDB information51039 52119
Descriptor28S ribosomal protein S34, mitochondrial, 28S ribosomal protein S2, mitochondrial, 28S ribosomal protein S24, mitochondrial, ... (41 entities in total)
Functional Keywordsmitochondrial ribosomal small subunit, translation-initiation intermediate, immature h44, single-particle cryo-em, ribosome
Biological sourceHomo sapiens (human)
More
Total number of polymer chains34
Total formula weight1249975.61
Authors
Finke, A.F.,Heinrichs, M.,Aibara, S.,Richter-Dennerlein, R.,Hillen, H.S. (deposition date: 2024-11-18, release date: 2025-04-23, Last modification date: 2025-04-30)
Primary citationHeinrichs, M.,Finke, A.F.,Aibara, S.,Krempler, A.,Boshnakovska, A.,Rehling, P.,Hillen, H.S.,Richter-Dennerlein, R.
Coupling of ribosome biogenesis and translation initiation in human mitochondria.
Nat Commun, 16:3641-3641, 2025
Cited by
PubMed Abstract: Biogenesis of mitoribosomes requires dedicated chaperones, RNA-modifying enzymes, and GTPases, and defects in mitoribosome assembly lead to severe mitochondriopathies in humans. Here, we characterize late-step assembly states of the small mitoribosomal subunit (mtSSU) by combining genetic perturbation and mutagenesis analysis with biochemical and structural approaches. Isolation of native mtSSU biogenesis intermediates via a FLAG-tagged variant of the GTPase MTG3 reveals three distinct assembly states, which show how factors cooperate to mature the 12S rRNA. In addition, we observe four distinct primed initiation mtSSU states with an incompletely matured rRNA, suggesting that biogenesis and translation initiation are not mutually exclusive processes but can occur simultaneously. Together, these results provide insights into mtSSU biogenesis and suggest a functional coupling between ribosome biogenesis and translation initiation in human mitochondria.
PubMed: 40240327
DOI: 10.1038/s41467-025-58827-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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PDB entries from 2025-05-28

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