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9ZRG

Structure of naked mole-rat ribosome (non-rotated)

This is a non-PDB format compatible entry.
Summary for 9ZRG
Entry DOI10.2210/pdb9zrg/pdb
EMDB information74615
Descriptor40S ribosomal protein S14, 40S ribosomal protein S27, Ubiquitin-like protein FUBI, ... (81 entities in total)
Functional Keywordsnaked mole rat ribosome, ribosome
Biological sourceHeterocephalus glaber
More
Total number of polymer chains82
Total formula weight4576638.50
Authors
Gutierrez-Vargas, C.,De, S.,Maji, S.,Liu, Z.,Nieb, M.,Seluanov, A.,Gorbunova, V.,Frank, J. (deposition date: 2025-12-19, release date: 2026-02-18)
Primary citationGutierrez-Vargas, C.,De, S.,Maji, S.,Liu, Z.,Ke, Z.,Niess, M.,Seluanov, A.,Gorbunova, V.,Frank, J.
Structures of naked mole-rat, tuco-tuco, and guinea pig ribosomes-is rRNA fragmentation linked to translational fidelity?
Nucleic Acids Res., 54:-, 2026
Cited by
PubMed Abstract: Ribosomes are central to protein synthesis in all organisms. In mammals, the ribosome functional core is highly conserved. Remarkably, two rodent species, the naked mole-rat (NMR) and tuco-tuco, display fragmented 28S ribosomal RNA (rRNA), coupled with high translational fidelity and long lifespan. The unusual ribosomal architecture in the NMR and tuco-tuco has been speculated to be linked to high translational fidelity. Here, we show, by single-particle cryo-electron microscopy, that despite the fragmentation of their rRNA, NMR and tuco-tuco ribosomes retain their core functional architecture. Compared to ribosomes of the guinea pig, a phylogenetically related rodent without 28S rRNA fragmentation, ribosomes of NMR and tuco-tuco exhibit poorly resolved density for certain expansion segments. In contrast, the structure of the guinea pig ribosome shows high similarity to the human ribosome. Enhanced translational fidelity in the NMR and tuco-tuco may stem from subtle, allosteric effects in dynamics, linked to rRNA fragmentation.
PubMed: 41603730
DOI: 10.1093/nar/gkag006
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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