8OM4

Small subunit of yeast mitochondrial ribosome.

This is a non-PDB format compatible entry.

Summary for 8OM4

• Entry DOI: 10.2210/pdb8om4/pdb
• EMDB information: 16968 17098 17099 17100 17101 17102
• Descriptor: 37S ribosomal protein MRP51, mitochondrial, 37S ribosomal protein S10, mitochondrial, 37S ribosomal protein S18, mitochondrial, ... (39 entities in total)
• Functional Keywords: mitochondria, ribosome
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 34
• Total formula weight: 1471353.73

Authors

Itoh, Y.,Chicherin, I.,Kamenski, P.,Amunts, A. (deposition date: 2023-03-31, release date: 2024-01-10, Last modification date: 2024-11-13)

Primary citation

Ast, T.,Itoh, Y.,Sadre, S.,McCoy, J.G.,Namkoong, G.,Wengrod, J.C.,Chicherin, I.,Joshi, P.R.,Kamenski, P.,Suess, D.L.M.,Amunts, A.,Mootha, V.K.
METTL17 is an Fe-S cluster checkpoint for mitochondrial translation.
Mol.Cell, 84:359-, 2024

PubMed Abstract: Friedreich's ataxia (FA) is a debilitating, multisystemic disease caused by the depletion of frataxin (FXN), a mitochondrial iron-sulfur (Fe-S) cluster biogenesis factor. To understand the cellular pathogenesis of FA, we performed quantitative proteomics in FXN-deficient human cells. Nearly every annotated Fe-S cluster-containing protein was depleted, indicating that as a rule, cluster binding confers stability to Fe-S proteins. We also observed depletion of a small mitoribosomal assembly factor METTL17 and evidence of impaired mitochondrial translation. Using comparative sequence analysis, mutagenesis, biochemistry, and cryoelectron microscopy, we show that METTL17 binds to the mitoribosomal small subunit during late assembly and harbors a previously unrecognized [FeS] cluster required for its stability. METTL17 overexpression rescued the mitochondrial translation and bioenergetic defects, but not the cellular growth, of FXN-depleted cells. These findings suggest that METTL17 acts as an Fe-S cluster checkpoint, promoting translation of Fe-S cluster-rich oxidative phosphorylation (OXPHOS) proteins only when Fe-S cofactors are replete.

PubMed: 38199006
DOI: 10.1016/j.molcel.2023.12.016

Experimental method

ELECTRON MICROSCOPY (2.32 Å)