Hilander, T;
Awadhpersad, R;
Monteuuis, G;
Broda, KL;
Pohjanpelto, M;
Pyman, E;
Singh, SK;
Nyman, TA;
Crevel, I;
Taylor, RW;
et al.
Hilander, T; Awadhpersad, R; Monteuuis, G; Broda, KL; Pohjanpelto, M; Pyman, E; Singh, SK; Nyman, TA; Crevel, I; Taylor, RW; Saada, A; Balboa, D; Battersby, BJ; Jackson, CB; Carroll, CJ
(2024)
Supernumerary proteins of the human mitochondrial ribosomal small subunit are integral for assembly and translation.
iScience, 27 (7).
p. 110185.
ISSN 2589-0042
https://doi.org/10.1016/j.isci.2024.110185
SGUL Authors: Carroll, Christopher John
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Abstract
Mitochondrial ribosomes (mitoribosomes) have undergone substantial evolutionary structural remodeling accompanied by loss of ribosomal RNA, while acquiring unique protein subunits located on the periphery. We generated CRISPR-mediated knockouts of all 14 unique (mitochondria-specific/supernumerary) human mitoribosomal proteins (snMRPs) in the small subunit to study the effect on mitoribosome assembly and protein synthesis, each leading to a unique mitoribosome assembly defect with variable impact on mitochondrial protein synthesis. Surprisingly, the stability of mS37 was reduced in all our snMRP knockouts of the small and large ribosomal subunits and patient-derived lines with mitoribosome assembly defects. A redox-regulated CX9C motif in mS37 was essential for protein stability, suggesting a potential mechanism to regulate mitochondrial protein synthesis. Together, our findings support a modular assembly of the human mitochondrial small ribosomal subunit mediated by essential supernumerary subunits and identify a redox regulatory role involving mS37 in mitochondrial protein synthesis in health and disease.
Item Type: | Article | |||||||||||||||||||||||||||
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Additional Information: | © 2024 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). | |||||||||||||||||||||||||||
Keywords: | biochemistry, biological sciences, cell biology, molecular biology | |||||||||||||||||||||||||||
SGUL Research Institute / Research Centre: | Academic Structure > REF 2021 user group | |||||||||||||||||||||||||||
Journal or Publication Title: | iScience | |||||||||||||||||||||||||||
ISSN: | 2589-0042 | |||||||||||||||||||||||||||
Language: | eng | |||||||||||||||||||||||||||
Dates: |
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Publisher License: | Creative Commons: Attribution 4.0 | |||||||||||||||||||||||||||
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PubMed ID: | 39015150 | |||||||||||||||||||||||||||
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URI: | https://openaccess.sgul.ac.uk/id/eprint/116685 | |||||||||||||||||||||||||||
Publisher's version: | https://doi.org/10.1016/j.isci.2024.110185 |
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