ArticleNucleic acids research2018
The regulon of the RNA chaperone CspA and its auto-regulation in Staphylococcus aureus.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 58 citations in OpenAlex.
- The RNA structural code: orchestrating gene expression and enabling precision therapies.Acta pharmacologica Sinica · 2026Review
- A family of RRM-1 RNA binding proteins enables cold adaptation and environmental resilience inbioRxiv : the preprint server for biology · 2026Article
- Unique structural and ligand-binding properties of theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- 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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- Unique structural and ligand binding properties of thebioRxiv : the preprint server for biology · 2025Article
- Cold Shock Proteins Balance Biofilm-Associated Antibiotic Resistance and Oxidative Vulnerability in Mycobacteria.Microorganisms · 2025Article
- An internal loop region is responsible for inherent target specificity of bacterial cold-shock proteins.RNA (New York, N.Y.) · 2024Article
- Lipidomics of homeoviscous adaptation to low temperatures inJournal of bacteriology · 2024Article
- Lipidomics of homeoviscous adaptation to low temperatures inbioRxiv : the preprint server for biology · 2024Article
- From Stress Tolerance to Virulence: Recognizing the Roles of Csps in Pathogenicity and Food Contamination.Pathogens (Basel, Switzerland) · 2024Review
- Unveiling the orchestration: mycobacterial small RNAs as key mediators in host-pathogen interactions.Frontiers in microbiology · 2024Review
- Effect of Essential Oil fromAntibiotics (Basel, Switzerland) · 2023Article
- The potential of cold-shock promoters for the expression of recombinant proteins in microbes and mammalian cells.Journal, genetic engineering & biotechnology · 2022Review
- Acetylation of CspC Controls the Las Quorum-Sensing System through Translational Regulation ofmBio · 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
- Article
- How global RNA-binding proteins coordinate the behaviour of RNA regulons: An information approach.Computational and structural biotechnology journal · 2022Article
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Authors and funding
12 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA-binding proteins (RBPs) are essential to fine-tune gene expression. RBPs containing the cold-shock domain are RNA chaperones that have been extensively studied. However, the RNA targets and specific functions for many of them remain elusive. Here, combining comparative proteomics and RBP-immunoprecipitation-microarray profiling, we have determined the regulon of the RNA chaperone CspA of Staphylococcus aureus. Functional analysis revealed that proteins involved in carbohydrate and ribonucleotide metabolism, stress response and virulence gene expression were affected by cspA deletion. Stress-associated phenotypes such as increased bacterial aggregation and diminished resistance to oxidative-stress stood out. Integration of the proteome and targetome showed that CspA post-transcriptionally modulates both positively and negatively the expression of its targets, denoting additional functions to the previously proposed translation enhancement. One of these repressed targets was its own mRNA, indicating the presence of a negative post-transcriptional feedback loop. CspA bound the 5'UTR of its own mRNA disrupting a hairpin, which was previously described as an RNase III target. Thus, deletion of the cspA 5'UTR abrogated mRNA processing and auto-regulation. We propose that CspA interacts through a U-rich motif, which is located at the RNase III cleavage site, portraying CspA as a putative RNase III-antagonist.
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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.