EMD-17094

Single-particle
2.87 Å
EMD-17094 Deposition: 11/04/2023
Map released: 10/01/2024
Last modified: 31/01/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-17094

Small subunit of yeast mitochondrial ribosome in complex with IF3/Aim23 (overall refinement)

EMD-17094

Single-particle
2.87 Å
EMD-17094 Deposition: 11/04/2023
Map released: 10/01/2024
Last modified: 31/01/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae
Sample: Small subunit of mitochondrial ribosome in complex with IF3/Aim23

Deposition Authors: Itoh Y , Chicherin I, Kamenski P, Amunts A
METTL17 is an Fe-S cluster checkpoint for mitochondrial translation.
PUBMED: 38199006
DOI: doi:10.1016/j.molcel.2023.12.016
ISSN: 1097-2765
ASTM: MOCEFL
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 [Fe4S4]2+ 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.