1. Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes
- Author
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André Schneider, Céline Prange, Elke K. Horn, Philipp Bieri, Daniel Boehringer, Marc Leibundgut, David J. F. Ramrath, Alexander Leitner, Moritz Niemann, and Nenad Ban
- Subjects
0301 basic medicine ,Models, Molecular ,Ribosomal Proteins ,Multidisciplinary ,biology ,Chemistry ,Trypanosoma brucei brucei ,Protozoan Proteins ,RNA ,Mitochondrion ,Trypanosoma brucei ,Ribosomal RNA ,biology.organism_classification ,Ribosome ,Cell biology ,Evolution, Molecular ,Mitochondrial Ribosomes ,03 medical and health sciences ,030104 developmental biology ,RNA, Ribosomal ,540 Chemistry ,Mitochondrial ribosome ,570 Life sciences - 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
- Published
- 2018