ArticleScientific reports2018
Structures of Mycobacterium smegmatis 70S ribosomes in complex with HPF, tmRNA, and P-tRNA.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
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- Role of starvation survival response mechanisms on ribosome integrity, antibiotic tolerances, and virulence of Pseudomonas aeruginosa biofilms.NPJ biofilms and microbiomes · 2026Article
- Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Future Research Directions on Mycobacterium tuberculosis Proteins.Advances in experimental medicine and biology · 2026Review
- Alternative ribosome expression alone is insufficient to drive antibiotic tolerance inFrontiers in microbiology · 2026Article
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- Structural studies of ribosome from an anaerobic Bacteroidetes human pathogen Porphyromonas gingivalis.Nucleic acids research · 2025Article
- Cryo- EM structure of the mycobacterial 70S ribosome in complex with ribosome hibernation promotion factor RafH.Nature communications · 2024Article
- Development of 2nd generation aminomethyl spectinomycins that overcome native efflux inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon.Frontiers in microbiology · 2024Article
- The structure of a hibernating ribosome in a Lyme disease pathogen.Nature communications · 2023Article
- Interactions between terminal ribosomal RNA helices stabilize theRNA (New York, N.Y.) · 2023Article
- Cryo-EM structure ofEmerging microbes & infections · 2022Article
- Ribosome profiling enhances understanding of mycobacterial translation.Frontiers in microbiology · 2022Review
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- Recent Insights into the Structure and Function of Mycobacterial Membrane Proteins Facilitated by Cryo-EM.The Journal of membrane biology · 2021Review
- A snapshot of translation in Mycobacterium tuberculosis during exponential growth and nutrient starvation revealed by ribosome profiling.Cell reports · 2021Article
- Ribosome hibernation: a new molecular framework for targeting nonreplicating persisters of mycobacteria.Microbiology (Reading, England) · 2021Review
- Role of Hibernation Promoting Factor in Ribosomal Protein Stability duringInternational journal of molecular sciences · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Ribosomes are the dynamic protein synthesis machineries of the cell. They may exist in different functional states in the cell. Therefore, it is essential to have structural information on these different functional states of ribosomes to understand their mechanism of action. Here, we present single particle cryo-EM reconstructions of the Mycobacterium smegmatis 70S ribosomes in the hibernating state (with HPF), trans-translating state (with tmRNA), and the P/P state (with P-tRNA) resolved to 4.1, 12.5, and 3.4 Å, respectively. A comparison of the P/P state with the hibernating state provides possible functional insights about the Mycobacteria-specific helix H54a rRNA segment. Interestingly, densities for all the four OB domains of bS1 protein is visible in the hibernating 70S ribosome displaying the molecular details of bS1-70S interactions. Our structural data shows a Mycobacteria-specific H54a-bS1 interaction which seems to prevent subunit dissociation and degradation during hibernation without the formation of 100S dimer. This indicates a new role of bS1 protein in 70S protection during hibernation in Mycobacteria in addition to its conserved function during translation initiation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.