ArticleNature communications2018
Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 46 citations in OpenAlex.
- Structure of the hibernating Francisella tularensis ribosome and mechanistic insights into its inhibition by antibiotics.Nucleic acids research · 2026Article
- Chloroplast Hibernation-Promoting Factor PSRP1 Prevents Ribosome Degradation Under Darkness Independently of 100S Dimer Formation.Plants (Basel, Switzerland) · 2025Article
- Draft genome sequences ofMicrobiology resource announcements · 2025Article
- Novel archaeal ribosome dimerization factor facilitating unique 30S-30S dimerization.Nucleic acids research · 2025Article
- Staphylococcal exoribonuclease YhaM destabilizes ribosomes by targeting the mRNA of a hibernation factor.Nucleic acids research · 2024Article
- Cryo- EM structure of the mycobacterial 70S ribosome in complex with ribosome hibernation promotion factor RafH.Nature communications · 2024Article
- The structure of a hibernating ribosome in a Lyme disease pathogen.Nature communications · 2023Article
- The Discovery of Ribosomal Protein bL31 fromInternational journal of molecular sciences · 2023Review
- Bidirectional sequestration between a bacterial hibernation factor and a glutamate metabolizing protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Interpretation of anomalously long crosslinks in ribosome crosslinking reveals the ribosome interaction in stationary phaseRSC chemical biology · 2022Article
- Amyloidogenic Peptides: New Class of Antimicrobial Peptides with the Novel Mechanism of Activity.International journal of molecular sciences · 2022Review
- Annealing synchronizes the 70Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Ribosome profiling enhances understanding of mycobacterial translation.Frontiers in microbiology · 2022Review
- Ribosomal Hibernation-Associated Factors inMicroorganisms · 2021Review
- Maturation of 23S rRNA includes removal of helix H1 in many bacteria.RNA biology · 2021Article
- The diversity of Shine-Dalgarno sequences sheds light on the evolution of translation initiation.RNA biology · 2021Review
- Hibernation factors directly block ribonucleases from entering the ribosome in response to starvation.Nucleic acids research · 2021Article
- Ribosome hibernation: a new molecular framework for targeting nonreplicating persisters of mycobacteria.Microbiology (Reading, England) · 2021Review
- Purification of Hibernating and Active C- Ribosomes from Zinc-Starved Mycobacteria.Methods in molecular biology (Clifton, N.J.) · 2021Article
- The conserved translation factor LepA is required for optimal synthesis of a porin family inJournal of bacteriology · 2020Article
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
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.
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