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Updated: Feb 5, 2026

Immunodetection of Outer Membrane Proteins by Flow Cytometry of Isolated Mitochondria
Published on: September 18, 2014
From powerhouse to processing plant: conserved roles of mitochondrial outer membrane proteins in tRNA splicing
Yao Wan1,2,3, Anita K Hopper1,2
1Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210, USA.
Abstract:
The mitochondrial cytoplasmic surface serves as a processing site for numerous RNAs from budding yeast to metazoans. We report that budding yeast mitochondrial outer membrane (MOM) proteins that are subunits of the translocase of the outer mitochondrial membrane (Tom70 and Tom 22) and sorting and assembly machinery (Sam37) are required for efficient pretransfer RNA (pre-tRNA) splicing. Defective pre-tRNA splicing in MOM mutants is due not to loss of respiratory metabolism but instead inefficient targeting/tethering of tRNA splicing endonuclease (SEN) subunits to mitochondria. Schizosaccharomyces pombe SEN subunits also localize to mitochondria, and Tom70 is required for this localization and pre-tRNA splicing. Thus, the role of MOM protein in targeting/tethering SEN subunits to mitochondria has been conserved for >500 million years.
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