The ribosome receptors Mrx15 and Mba1 jointly organize cotranslational insertion and protein biogenesis in mitochondria
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Updated: Feb 6, 2026

Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs
Published on: November 19, 2020
Braulio Vargas Möller-Hergt1, Andreas Carlström1, Katharina Stephan1
1Department of Biochemistry and Biophysics, Stockholm University, SE-10691 Stockholm, Sweden.
Abstract:
Mitochondrial gene expression in Saccharomyces cerevisiae is responsible for the production of highly hydrophobic subunits of the oxidative phosphorylation system. Membrane insertion occurs cotranslationally on membrane-bound mitochondrial ribosomes. Here, by employing a systematic mass spectrometry-based approach, we discovered the previously uncharacterized membrane protein Mrx15 that interacts via a soluble C-terminal domain with the large ribosomal subunit. Mrx15 contacts mitochondrial translation products during their synthesis and plays, together with the ribosome receptor Mba1, an overlapping role in cotranslational protein insertion. Taken together, our data reveal how these ribosome receptors organize membrane protein biogenesis in mitochondria.
Insights
Researchers discovered Mrx15, a new protein crucial for mitochondrial membrane protein insertion. This protein works with Mba1 to ensure proper biogenesis of oxidative phosphorylation system components.
Area of Science:
- Mitochondrial biology
- Molecular cell biology
- Protein biogenesis
Background:
- Mitochondrial gene expression produces essential oxidative phosphorylation subunits.
- These hydrophobic proteins require cotranslational insertion into the inner mitochondrial membrane.
- Membrane insertion occurs on mitochondrial ribosomes.
Purpose of the Study:
- To identify novel factors involved in mitochondrial cotranslational protein insertion.
- To elucidate the mechanism of membrane protein biogenesis in mitochondria.
Main Methods:
- Systematic mass spectrometry-based proteomic approach.
- Identification and characterization of novel interacting partners of mitochondrial ribosomes.
Main Results:
- Discovery of a previously uncharacterized membrane protein, Mrx15.
- Mrx15 interacts with the large ribosomal subunit via its C-terminal domain.
- Mrx15 contacts nascent mitochondrial translation products.
- Mrx15 and Mba1 play overlapping roles in cotranslational protein insertion.
Conclusions:
- Mrx15 is a novel ribosome receptor involved in mitochondrial membrane protein biogenesis.
- Ribosome receptors like Mrx15 and Mba1 organize the cotranslational insertion of proteins into the mitochondrial inner membrane.
- This study reveals a new mechanism for organizing mitochondrial membrane protein biogenesis.
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