MR-1S Interacts with PET100 and PET117 in Module-Based Assembly of Human Cytochrome c Oxidase.

TitleMR-1S Interacts with PET100 and PET117 in Module-Based Assembly of Human Cytochrome c Oxidase.
Publication TypeJournal Article
Year of Publication2017
AuthorsVidoni, S, Harbour, ME, Guerrero-Castillo, S, Signes, A, Ding, S, Fearnley, IM, Taylor, RW, Tiranti, V, Arnold, S, Fernandez-Vizarra, E, Zeviani, M
JournalCell Rep
Volume18
Issue7
Pagination1727-1738
Date Published2017 Feb 14
ISSN2211-1247
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.

DOI10.1016/j.celrep.2017.01.044
Alternate JournalCell Rep
Citation Key10.1016/j.celrep.2017.01.044
PubMed ID28199844
Grant ListMC_UP_1002/1 / / Medical Research Council / United Kingdom