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

Lookup NU author(s): Professor Robert Taylor

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This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (CC BY-NC-ND).


Abstract

© 2017 Elsevier Inc. 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.


Publication metadata

Author(s): Vidoni S, Harbour ME, Guerrero-Castillo S, Signes A, Ding S, Fearnley IM, Taylor RW, Tiranti V, Arnold S, Fernandez-Vizarra E, Zeviani M

Publication type: Article

Publication status: Published

Journal: Cell Reports

Year: 2017

Volume: 18

Issue: 7

Pages: 1727-1738

Print publication date: 14/02/2017

Online publication date: 14/02/2017

Acceptance date: 19/01/2017

ISSN (electronic): 2211-1247

Publisher: Elsevier BV

URL: https://doi.org/10.1016/j.celrep.2017.01.044

DOI: 10.1016/j.celrep.2017.01.044


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