ArticleJournal of bacteriology2015
The Listeria monocytogenes hibernation-promoting factor is required for the formation of 100S ribosomes, optimal fitness, and pathogenesis.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Role of starvation survival response mechanisms on ribosome integrity, antibiotic tolerances, and virulence of Pseudomonas aeruginosa biofilms.NPJ biofilms and microbiomes · 2026Article
- Review
- Regulation of ribosome hibernation controlsmBio · 2026Article
- Chloroplast Hibernation-Promoting Factor PSRP1 Prevents Ribosome Degradation Under Darkness Independently of 100S Dimer Formation.Plants (Basel, Switzerland) · 2025Article
- Staphylococcal exoribonuclease YhaM destabilizes ribosomes by targeting the mRNA of a hibernation factor.Nucleic acids research · 2024Article
- 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
- Ribosome profiling enhances understanding of mycobacterial translation.Frontiers in microbiology · 2022Review
- Article
- Transcription regulates ribosome hibernation.Molecular microbiology · 2021Article
- Listeria monocytogenes MenI Encodes a DHNA-CoA Thioesterase Necessary for Menaquinone Biosynthesis, Cytosolic Survival, and Virulence.Infection and immunity · 2021Article
- Hibernation factors directly block ribonucleases from entering the ribosome in response to starvation.Nucleic acids research · 2021Article
- High-pressure processing-induced transcriptome response during recovery of Listeria monocytogenes.BMC genomics · 2021Article
- Ribosome hibernation: a new molecular framework for targeting nonreplicating persisters of mycobacteria.Microbiology (Reading, England) · 2021Review
- Progression from remodeling to hibernation of ribosomes in zinc-starved mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The hibernating 100S complex is a target of ribosome-recycling factor and elongation factor G inThe Journal of biological chemistry · 2020Article
- Ribosome Dimerization Protects the Small Subunit.Journal of bacteriology · 2020Article
- Stress response as implemented by hibernating ribosomes: a structural overview.The FEBS journal · 2019Review
- Lag Phase Is a Dynamic, Organized, Adaptive, and Evolvable Period That Prepares Bacteria for Cell Division.Journal of bacteriology · 2019Review
- Thermal and Nutritional Regulation of Ribosome Hibernation in Staphylococcus aureus.Journal of bacteriology · 2018Article
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4 authors.
Funding
Abstract
During exposure to certain stresses, bacteria dimerize pairs of 70S ribosomes into translationally silent 100S particles in a process called ribosome hibernation. Although the biological roles of ribosome hibernation are not completely understood, this process appears to represent a conserved and adaptive response that contributes to optimal survival during stress and post-exponential-phase growth. Hibernating ribosomes are formed by the activity of one or more highly conserved proteins; gammaproteobacteria produce two relevant proteins, ribosome modulation factor (RMF) and hibernation promoting factor (HPF), while most Gram-positive bacteria produce a single, longer HPF protein. Here, we report the formation of 100S ribosomes by an HPF homolog in Listeria monocytogenes. L. monocytogenes 100S ribosomes were observed by sucrose density gradient centrifugation of bacterial extracts during mid-logarithmic phase, peaked at the transition to stationary phase, and persisted at lower levels during post-exponential-phase growth. 100S ribosomes were undetectable in bacteria carrying an hpf::Himar1 transposon insertion, indicating that HPF is required for ribosome hibernation in L. monocytogenes. Additionally, epitope-tagged HPF cosedimented with 100S ribosomes, supporting its previously described direct role in 100S formation. We examined hpf mRNA by quantitative PCR (qPCR) and identified several conditions that upregulated its expression, including carbon starvation, heat shock, and exposure to high concentrations of salt or ethanol. Survival of HPF-deficient bacteria was impaired under certain conditions both in vitro and during animal infection, providing evidence for the biological relevance of 100S ribosome formation.
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