ArticleNucleic acids research2021
RNA thermoswitches modulate Staphylococcus aureus adaptation to ambient temperatures.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- A 5'-UTR cis-acting RNA element targeted by RNase III is essential for DNA simple sequence repeat-dependent phase variation in Haemophilus influenzae.Nucleic acids research · 2025Article
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- Integrating temperature into the Arabidopsis circadian system.Npj biological timing and sleep · 2025Review
- Fever-like temperature impacts on Staphylococcus aureus and Pseudomonas aeruginosa interaction, physiology, and virulence both in vitro and in vivo.BMC biology · 2024Article
- The canonical single-stranded DNA-binding protein is not an essential replication factor but an RNA chaperon iniScience · 2023Article
- Multilayer Regulation ofMicroorganisms · 2022Article
- Comparative Transcriptomic Analysis ofFoods (Basel, Switzerland) · 2022Article
- Regulation of Heterogenous LexA Expression inInternational journal of molecular sciences · 2022Article
- Deciphering the global roles of Cold shock proteins inFrontiers in microbiology · 2022Article
- A General Map of Transcriptional Expression of Virulence, Metabolism, and Biofilm Formation Adaptive Changes ofFrontiers in microbiology · 2022Article
- Functional Redundancy and Specialization of the Conserved Cold Shock Proteins inMicroorganisms · 2021Article
- Review
- Diversity and Versatility in Small RNA-Mediated Regulation in Bacterial Pathogens.Frontiers in microbiology · 2021Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermoregulation of virulence genes in bacterial pathogens is essential for environment-to-host transition. However, the mechanisms governing cold adaptation when outside the host remain poorly understood. Here, we found that the production of cold shock proteins CspB and CspC from Staphylococcus aureus is controlled by two paralogous RNA thermoswitches. Through in silico prediction, enzymatic probing and site-directed mutagenesis, we demonstrated that cspB and cspC 5'UTRs adopt alternative RNA structures that shift from one another upon temperature shifts. The open (O) conformation that facilitates mRNA translation is favoured at ambient temperatures (22°C). Conversely, the alternative locked (L) conformation, where the ribosome binding site (RBS) is sequestered in a double-stranded RNA structure, is folded at host-related temperatures (37°C). These structural rearrangements depend on a long RNA hairpin found in the O conformation that sequesters the anti-RBS sequence. Notably, the remaining S. aureus CSP, CspA, may interact with a UUUGUUU motif located in the loop of this long hairpin and favour the folding of the L conformation. This folding represses CspB and CspC production at 37°C. Simultaneous deletion of the cspB/cspC genes or their RNA thermoswitches significantly decreases S. aureus growth rate at ambient temperatures, highlighting the importance of CspB/CspC thermoregulation when S. aureus transitions from the host to the environment.
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