Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Ribosomes hibernate on mitochondria during cellular stress.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 8666, Year 2024
Publish date	Oct 8, 2024
Authors	Olivier Gemin / Maciej Gluc / Higor Rosa / Michael Purdy / Moritz Niemann / Yelena Peskova / Simone Mattei / Ahmad Jomaa /
PubMed Abstract	Cell survival under nutrient-deprived conditions relies on cells' ability to adapt their organelles and rewire their metabolic pathways. In yeast, glucose depletion induces a stress response mediated ...Cell survival under nutrient-deprived conditions relies on cells' ability to adapt their organelles and rewire their metabolic pathways. In yeast, glucose depletion induces a stress response mediated by mitochondrial fragmentation and sequestration of cytosolic ribosomes on mitochondria. This cellular adaptation promotes survival under harsh environmental conditions; however, the underlying mechanism of this response remains unknown. Here, we demonstrate that upon glucose depletion protein synthesis is halted. Cryo-electron microscopy structure of the ribosomes show that they are devoid of both tRNA and mRNA, and a subset of the particles depicted a conformational change in rRNA H69 that could prevent tRNA binding. Our in situ structural analyses reveal that the hibernating ribosomes tether to fragmented mitochondria and establish eukaryotic-specific, higher-order storage structures by assembling into oligomeric arrays on the mitochondrial surface. Notably, we show that hibernating ribosomes exclusively bind to the outer mitochondrial membrane via the small ribosomal subunit during cellular stress. We identify the ribosomal protein Cpc2/RACK1 as the molecule mediating ribosomal tethering to mitochondria. This study unveils the molecular mechanism connecting mitochondrial stress with the shutdown of protein synthesis and broadens our understanding of cellular responses to nutrient scarcity and cell quiescence.
External links	Nat Commun / PubMed:39379376 / PubMed Central
Methods	EM (single particle) / EM (subtomogram averaging)
Resolution	1.94 - 14.64 Å
Structure data	EMDB-43970: Non-translating Schizosaccharomyces pombe ribosome large subunit Method: EM (single particle) / Resolution: 2.44 Å EMDB-43971: Non-translating Schizosaccharomyces pombe ribosome small subunit Method: EM (single particle) / Resolution: 2.96 Å 43972 9axt EMDB-43972, PDB-9axt: Non-translating S. pombe ribosome Method: EM (single particle) / Resolution: 2.4 Å 43973 9axu EMDB-43973, PDB-9axu: Non-translating S. pombe ribosome large subunit Method: EM (single particle) / Resolution: 1.94 Å EMDB-43974: Translating Schizosaccharomyces pombe ribosome small subunit Method: EM (single particle) / Resolution: 2.84 Å EMDB-43975: Translating Schizosaccharomyces pombe ribosome large subunit Method: EM (single particle) / Resolution: 2.41 Å 43976 9axv EMDB-43976, PDB-9axv: Translating S. pombe ribosome Method: EM (single particle) / Resolution: 2.4 Å EMDB-50266: Cytoplasmic Fission Yeast Ribosome Tethered to the Outer Mitochondrial Membrane Method: EM (subtomogram averaging) / Resolution: 11.4 Å EMDB-51002: Untethered Cytoplasmic Fission Yeast Ribosome Method: EM (subtomogram averaging) / Resolution: 14.64 Å EMDB-51030: Untethered Cytoplasmic Fission Yeast Ribosome (S. pombe) Method: EM (subtomogram averaging) / Resolution: 14.2 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry
Source	Schizosaccharomyces pombe 972h- (yeast) schizosaccharomyces pombe (fission yeast)
Keywords	RIBOSOME / Schizosaccharomyces pombe / protein synthesis / S. pombe / TRANSLATION / Non-translating / 60S / Large subunit / Schizosasccharomyces pombe / tRNA / mRNA