1. MR-1S Interacts with PET100 and PET117 in Module-Based Assembly of Human Cytochrome c Oxidase.
- Author
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Vidoni S, Harbour ME, Guerrero-Castillo S, Signes A, Ding S, Fearnley IM, Taylor RW, Tiranti V, Arnold S, Fernandez-Vizarra E, and Zeviani M
- Subjects
- Cell Line, Tumor, Cell Nucleus metabolism, Cells, Cultured, DNA, Mitochondrial genetics, Humans, Mitochondria genetics, Mitochondria metabolism, Molecular Chaperones metabolism, Protein Subunits metabolism, Adaptor Proteins, Signal Transducing metabolism, Electron Transport Complex IV metabolism, Mitochondrial Proteins metabolism, Muscle Proteins metabolism
- Abstract
The biogenesis of human cytochrome c oxidase (COX) is an intricate process in which three mitochondrial DNA (mtDNA)-encoded core subunits are assembled in a coordinated way with at least 11 nucleus-encoded subunits. Many chaperones shared between yeast and humans are involved in COX assembly. Here, we have used a MT-CO3 mutant cybrid cell line to define the composition of assembly intermediates and identify new human COX assembly factors. Quantitative mass spectrometry analysis led us to modify the assembly model from a sequential pathway to a module-based process. Each module contains one of the three core subunits, together with different ancillary components, including HIGD1A. By the same analysis, we identified the short isoform of the myofibrillogenesis regulator 1 (MR-1S) as a new COX assembly factor, which works with the highly conserved PET100 and PET117 chaperones to assist COX biogenesis in higher eukaryotes., (Copyright © 2017 Elsevier Inc. All rights reserved.)
- Published
- 2017
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