Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes

Author:

Ramrath David J. F.1ORCID,Niemann Moritz2ORCID,Leibundgut Marc1ORCID,Bieri Philipp1ORCID,Prange Céline1,Horn Elke K.2,Leitner Alexander3ORCID,Boehringer Daniel1,Schneider André2ORCID,Ban Nenad1ORCID

Affiliation:

1. Department of Biology, Institute of Molecular Biology and Biophysics, Otto-Stern-Weg 5, ETH Zurich, CH-8093 Zurich, Switzerland.

2. Department of Chemistry and Biochemistry, University of Bern, CH-3012 Bern, Switzerland.

3. Department of Biology, Institute of Molecular Systems Biology, Auguste-Piccard-Hof 1, ETH Zurich, CH-8093 Zurich, Switzerland.

Abstract

Structure of the largest, most complex ribosome Ribosomes are two-subunit ribonucleoprotein assemblies that catalyze the translation of messenger RNA into protein. Ribosomal RNAs (rRNAs) play key structural and functional roles. Ramrath et al. report the high-resolution structure of mitochondrial ribosomes from the unicellular parasite Trypanosoma brucei that contain the smallest known rRNAs. The trypanosomal mitoribosome is the most complex ribosomal assembly characterized, with two rRNAs and 126 proteins. The increased protein subunits have substituted for rRNA as an architectural scaffold. The structure also reveals the minimal core needed for ribosome function. Science , this issue p. eaau7735

Funder

Federation of European Biochemical Societies

Swiss National Science Foundation

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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