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Nat Commun. 2018 Oct 9;9(1):4179. doi: 10.1038/s41467-018-06724-x.

Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism.

Author information

1
Department of Molecular Biology and Genetics, Aarhus University, 8000, Aarhus C, Denmark.
2
Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, CNRS UMR710, INSERM U964, University of Strasbourg, Strasbourg, 67000, France.
3
Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan, 420008, Russia.
4
Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, CNRS UMR710, INSERM U964, University of Strasbourg, Strasbourg, 67000, France. lasse@igbmc.fr.

Abstract

In response to cellular stresses bacteria conserve energy by dimerization of ribosomes into inactive hibernating 100S ribosome particles. Ribosome dimerization in Thermus thermophilus is facilitated by hibernation-promoting factor (TtHPF). In this study we demonstrate high sensitivity of Tt100S formation to the levels of TtHPF and show that a 1:1 ratio leads to optimal dimerization. We report structures of the T. thermophilus 100S ribosome determined by cryo-electron microscopy to average resolutions of 4.13 Å and 4.57 Å. In addition, we present a 3.28 Å high-resolution cryo-EM reconstruction of a 70S ribosome from a hibernating ribosome dimer and reveal a role for the linker region connecting the TtHPF N- and C-terminal domains in translation inhibition by preventing Shine-Dalgarno duplex formation. Our work demonstrates that species-specific differences in the dimerization interface govern the overall conformation of the 100S ribosome particle and that for Thermus thermophilus no ribosome-ribosome interactions are involved in the interface.

PMID:
30301898
PMCID:
PMC6177447
DOI:
10.1038/s41467-018-06724-x
[Indexed for MEDLINE]
Free PMC Article

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