ArticleNucleic acids research2016
Ribosome hibernation factor promotes Staphylococcal survival and differentially represses translation.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Review
- Structural insights into RNA recognition by theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- Regulation of ribosome hibernation controlsmBio · 2026Article
- Article
- Chloroplast Hibernation-Promoting Factor PSRP1 Prevents Ribosome Degradation Under Darkness Independently of 100S Dimer Formation.Plants (Basel, Switzerland) · 2025Article
- In vivo virulence ofJTCVS open · 2025Article
- Functional and Proteomic Dissection of the Contributions of CodY, SigB and the Hibernation Promoting Factor HPF to Interactions ofJournal of proteome research · 2024Article
- Staphylococcal exoribonuclease YhaM destabilizes ribosomes by targeting the mRNA of a hibernation factor.Nucleic acids research · 2024Article
- Article
- Epitranscriptional m6A modification of rRNA negatively impacts translation and host colonization in Staphylococcus aureus.PLoS pathogens · 2024Article
- Article
- Article
- 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
- Article
- Absence of Ribosome Modulation Factor Alters Growth and Competitive Fitness of Escherichia coli.Microbiology spectrum · 2022Article
- Identifying Small Open Reading Frames in Prokaryotes with Ribosome Profiling.Journal of bacteriology · 2022Article
- Article
- Article
- Transcription regulates ribosome hibernation.Molecular microbiology · 2021Article
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Authors and funding
2 authors.
Funding
Abstract
In opportunistic Gram-positive Staphylococcus aureus, a small protein called hibernation-promoting factor (HPFSa) is sufficient to dimerize 2.5-MDa 70S ribosomes into a translationally inactive 100S complex. Although the 100S dimer is observed in only the stationary phase in Gram-negative gammaproteobacteria, it is ubiquitous throughout all growth phases in S. aureus The biological significance of the 100S ribosome is poorly understood. Here, we reveal an important role of HPFSa in preserving ribosome integrity and poising cells for translational restart, a process that has significant clinical implications for relapsed staphylococcal infections. We found that the hpf null strain is severely impaired in long-term viability concomitant with a dramatic loss of intact ribosomes. Genome-wide ribosome profiling shows that eliminating HPFSa drastically increased ribosome occupancy at the 5' end of specific mRNAs under nutrient-limited conditions, suggesting that HPFSa may suppress translation initiation. The protective function of HPFSa on ribosomes resides at the N-terminal conserved basic residues and the extended C-terminal segment, which are critical for dimerization and ribosome binding, respectively. These data provide significant insight into the functional consequences of 100S ribosome loss for protein synthesis and stress adaptation.
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