Journal
NUCLEIC ACIDS RESEARCH
Volume 48, Issue 20, Pages 11750-11761Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkaa893
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Funding
- ERC-PoC [862028]
- Weizmann-Krenter-Katz Interdisciplinary Research
- Zuckerman STEM Leadership Program
- Ilse Katz Institute for Material Sciences and Magnetic Resonance Research
- Helen & Milton A. Kimmelman Center for Biomolecular Structure Assembly
- Joseph and Wolf Lebovic Lab
- Dov and Ziva Rabinovich Endowed Fund for Structural Biology
- Harmstieg New Scientist Fund
- Pearl Welinsky Merlo Foundation
- Paul and Tina Gardner
- Natural Sciences and Engineering Research Council of Canada [NSERC A8387]
- Canadian Institutes of Health Research [CIHR MOP-11212]
- Clore Fellowship
- Japan Science and Technology Agency for Core Research for Evolutional Science and Technology [13415564]
- European Research Council (ERC) [862028] Funding Source: European Research Council (ERC)
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Ribosomal RNA is the central component of the ribosome, mediating its functional and architectural properties. Here, we report the cryo-EM structure of a highly divergent cytoplasmic ribosome from the single-celled eukaryotic alga Euglena gracilis. The Euglena large ribosomal subunit is distinct in that it contains 14 discrete rRNA fragments that are assembled non-covalently into the canonical ribosome structure. The rRNA is substantially enriched in post-transcriptional modifications that are spread far beyond the catalytic RNA core, contributing to the stabilization of this highly fragmented ribosome species. A unique cluster of five adenosine base methylations is found in an expansion segment adjacent to the protein exit tunnel, such that it is positioned for interaction with the nascent peptide. As well as featuring distinctive rRNA expansion segments, the Euglena ribosome contains four novel ribosomal proteins, localized to the ribosome surface, three of which do not have orthologs in other eukaryotes.
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