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Rapid Isolation of the Mitoribosome from HEK Cells
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Rapid Isolation of the Mitoribosome from HEK Cells

Published on: October 4, 2018

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The mitoribosome-specific protein mS38 is preferentially required for synthesis of cytochrome c oxidase subunits

Jeffri-Noelle Mays1, Yolanda Camacho-Villasana2, Rodolfo Garcia-Villegas2

  • 1Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.

Nucleic Acids Research
|April 11, 2019
PubMed

Insights

The mitochondrial ribosome protein Cox24/mS38 is crucial for efficient mitochondrial protein synthesis in yeast. Its absence disrupts the translation of key oxidative phosphorylation (OXPHOS) genes, suggesting a direct role for the mitoribosome in translational regulation.

Area of Science:

  • Mitochondrial biology
  • Molecular genetics
  • Yeast research

Background:

  • Mitochondrial protein synthesis relies on mitoribosomes and nucleus-encoded partners.
  • Message-specific translational activators coordinate oxidative phosphorylation (OXPHOS) enzyme biogenesis.
  • The mitoribosome's intrinsic role in translational regulation remains largely unexplored.

Purpose of the Study:

  • To investigate the function of the mitoribosome small subunit protein Cox24/mS38.
  • To determine the role of mS38 in mitoribogenesis and mitochondrial protein synthesis.
  • To elucidate the impact of mS38 absence on mRNA-specific translational regulation.

Main Methods:

  • Yeast genetics (Saccharomyces cerevisiae) to create mS38-deleted strains.
  • Analysis of mitoribosome abundance and mitochondrial protein synthesis rates.
  • Investigation of translation initiation for specific OXPHOS mRNAs (COX1, COX2, COX3).

Main Results:

  • Cox24/mS38 is essential for efficient mitoribogenesis and overall mitochondrial protein synthesis.
  • Mitoribosome abundance increases in mS38-deleted cells, but protein synthesis rates are not maintained.
  • Absence of mS38 specifically impairs translation initiation of COX1, COX2, and COX3 mRNAs.
  • Levels of mRNA-specific translational activators are unaffected by mS38 deletion.

Conclusions:

  • Mitochondrial ribosome protein mS38 confers an intrinsic translational regulatory capacity to the mitoribosome.
  • This regulatory function likely evolved from bacterial ribosomes to facilitate translation of mitochondrial mRNAs lacking typical Shine-Dalgarno sequences.
  • mS38 is critical for coordinating OXPHOS gene expression at the translational level.

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