Browse by author
Lookup NU author(s): Professor Robert Taylor
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2024 The AuthorsMitochondrial 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.
Author(s): 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
Publication type: Article
Publication status: Published
Journal: iScience
Year: 2024
Volume: 27
Issue: 7
Print publication date: 19/07/2024
Online publication date: 04/06/2024
Acceptance date: 01/06/2024
Date deposited: 04/07/2024
ISSN (electronic): 2589-0042
Publisher: Elsevier Inc.
URL: https://doi.org/10.1016/j.isci.2024.110185
DOI: 10.1016/j.isci.2024.110185
Data Access Statement: Data Data reported in this paper will be shared by the lead contact upon request. Mass-spectrometry proteomics data have been submitted to the ProteomeXchange Consortium via the PRIDE partner repository; Identifier: PXD034224. Code No original code has been generated in this study. Structural data No structural data has been generated in this study. Other Any additional information required to reanalyze the data reported in this paper is available from the lead contact upon request.
Altmetrics provided by Altmetric
