Mitoribosomal small subunit maturation involves formation of initiation-like complexes

Lenarčič, Tea; Niemann, Moritz; Ramrath, David J. F.; Calderaro, Salvatore; Flügel, Timo; Saurer, Martin; Leibundgut, Marc; Boehringer, Daniel; Prange, Céline; Horn, Elke K.; Schneider, André; Ban, Nenad (2022). Mitoribosomal small subunit maturation involves formation of initiation-like complexes. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 119(3), e2114710118. National Academy of Sciences NAS 10.1073/pnas.2114710118

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Mitochondrial ribosomes (mitoribosomes) play a central role in synthesizing mitochondrial inner membrane proteins responsible for oxidative phosphorylation. Although mitoribosomes from different organisms exhibit considerable structural variations, recent insights into mitoribosome assembly suggest that mitoribosome maturation follows common principles and involves a number of conserved assembly factors. To investigate the steps involved in the assembly of the mitoribosomal small subunit (mt-SSU) we determined the cryoelectron microscopy structures of middle and late assembly intermediates of the Trypanosoma brucei mitochondrial small subunit (mt-SSU) at 3.6- and 3.7-Å resolution, respectively. We identified five additional assembly factors that together with the mitochondrial initiation factor 2 (mt-IF-2) specifically interact with functionally important regions of the rRNA, including the decoding center, thereby preventing premature mRNA or large subunit binding. Structural comparison of assembly intermediates with mature mt-SSU combined with RNAi experiments suggests a noncanonical role of mt-IF-2 and a stepwise assembly process, where modular exchange of ribosomal proteins and assembly factors together with mt-IF-2 ensure proper 9S rRNA folding and protein maturation during the final steps of assembly.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)
08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP) > NCCR RNA & Disease

UniBE Contributor:

Niemann, Moritz, Calderaro, Salvatore, Horn Schneider, Elke Karin, Schneider, André

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

0027-8424

Publisher:

National Academy of Sciences NAS

Language:

English

Submitter:

Christina Schüpbach

Date Deposited:

15 Feb 2022 10:33

Last Modified:

28 Mar 2024 13:56

Publisher DOI:

10.1073/pnas.2114710118

PubMed ID:

35042777

BORIS DOI:

10.48350/164862

URI:

https://boris.unibe.ch/id/eprint/164862

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