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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Ribosomes hibernate on mitochondria during cellular stress.

Olivier Gemin1, Maciej Gluc2, Higor Rosa1

  • 1European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstraße 1, Heidelberg, Germany.

Nature Communications
|October 8, 2024
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Yeast cells halt protein synthesis and form hibernating ribosome-mitochondria complexes to survive nutrient scarcity. This involves ribosomes binding to mitochondria via Cpc2/RACK1, enabling cell quiescence.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Cellular adaptation to nutrient deprivation is crucial for survival.
  • Yeast exhibits mitochondrial fragmentation and ribosome sequestration upon glucose depletion.
  • The precise mechanism linking mitochondrial stress to protein synthesis shutdown is unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism of protein synthesis shutdown during nutrient stress in yeast.
  • To investigate the structural basis of ribosome-mitochondria interactions under starvation conditions.
  • To identify the factors mediating the tethering of hibernating ribosomes to mitochondria.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) for ribosome structure determination.
  • In situ structural analyses to visualize ribosome-mitochondria complexes.
  • Biochemical assays to identify protein interactions.

Main Results:

  • Glucose depletion halts protein synthesis, with ribosomes lacking tRNA and mRNA.
  • Hibernating ribosomes form higher-order oligomeric arrays on the outer mitochondrial membrane.
  • Ribosomal protein Cpc2/RACK1 mediates the tethering of ribosomes to mitochondria via the small ribosomal subunit.

Conclusions:

  • The study reveals a novel mechanism connecting mitochondrial stress to protein synthesis inhibition.
  • Hibernating ribosomes are stored on mitochondria through specific protein interactions, facilitating cell quiescence.
  • This provides insights into cellular responses to nutrient scarcity and the regulation of protein synthesis.