MRPS27 is a pentatricopeptide repeat domain protein required for the translation of mitochondrially encoded proteins
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Updated: May 20, 2026

Rapid Isolation of the Mitoribosome from HEK Cells
Published on: October 4, 2018
Stefan M K Davies1, Maria I G Lopez Sanchez, Reena Narsai
1Western Australian Institute for Medical Research and Centre for Medical Research, The University of Western Australia, Perth, Western Australia 6000, Australia.
Abstract:
Mammalian pentatricopeptide repeat domain (PPR) proteins are involved in regulation of mitochondrial RNA metabolism and translation and are required for mitochondrial function. We investigated an uncharacterised PPR protein, the supernumerary mitochondrial ribosomal protein of the small subunit 27 (MRPS27), and show that it associates with the 12S rRNA and tRNA(Glu), however it does not affect their abundance. We found that MRPS27 is not required for mitochondrial RNA processing or the stability of the small ribosomal subunit. However, MRPS27 is required for mitochondrial protein synthesis and its knockdown causes decreased abundance in respiratory complexes and cytochrome c oxidase activity.
Insights
Supernumerary mitochondrial ribosomal protein 27 (MRPS27) associates with mitochondrial RNA but is not essential for RNA processing. MRPS27 is crucial for mitochondrial protein synthesis, impacting respiratory complexes and enzyme activity.
Area of Science:
- Mitochondrial biology
- Molecular genetics
- Protein synthesis
Background:
- Pentatricopeptide repeat (PPR) proteins regulate mitochondrial RNA metabolism and translation.
- Mitochondrial function relies on proper RNA metabolism and protein synthesis.
- The role of uncharacterized PPR proteins like MRPS27 in mitochondrial function is largely unknown.
Purpose of the Study:
- To investigate the function of the uncharacterized PPR protein, supernumerary mitochondrial ribosomal protein of the small subunit 27 (MRPS27).
- To determine MRPS27's role in mitochondrial RNA metabolism, ribosomal subunit stability, and protein synthesis.
Main Methods:
- Investigated MRPS27's association with mitochondrial 12S rRNA and tRNA(Glu).
- Assessed the impact of MRPS27 knockdown on mitochondrial RNA processing and ribosomal subunit stability.
- Evaluated MRPS27's requirement for mitochondrial protein synthesis and its effect on respiratory complexes.
Main Results:
- MRPS27 associates with 12S rRNA and tRNA(Glu) without affecting their abundance.
- MRPS27 is not required for mitochondrial RNA processing or small ribosomal subunit stability.
- MRPS27 is essential for mitochondrial protein synthesis; its knockdown reduces respiratory complexes and cytochrome c oxidase activity.
Conclusions:
- MRPS27 plays a vital role in mitochondrial protein synthesis, not RNA processing.
- Dysfunction of MRPS27 impairs mitochondrial respiration by affecting protein synthesis and complex assembly.
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