ArticlePloS one2010
The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- Unraveling proteomic chaos by independent component analysis-ClpX proficiency promotes the iron and oxygen limitation responses ofmSystems · 2025Article
- Discovery of coniferaldehyde as an inhibitor of caseinolytic protease to combat Staphylococcus aureus infections.Molecular medicine (Cambridge, Mass.) · 2025Article
- The ClpX protease is essential for inactivating the CI master repressor and completing prophage induction in Staphylococcus aureus.Nature communications · 2023Article
- Molecular Determinants of β-Lactam Resistance in Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2023Review
- Global transcriptomic response of the AI-3 isomers 3,5-DPO and 3,6-DPO in Salmonella Typhimurium.Archives of microbiology · 2023Article
- An Interplay of Multiple Positive and Negative Factors Governs Methicillin Resistance in Staphylococcus aureus.Microbiology and molecular biology reviews : MMBR · 2022Review
- Staphylococcal ClpXP protease targets the cellular antioxidant system to eliminate fitness-compromised cells in stationary phase.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- AFrontiers in molecular biosciences · 2021Article
- Deletion ofInfection and drug resistance · 2021Article
- Article
- Staphylococcus aureus ClpX localizes at the division septum and impacts transcription of genes involved in cell division, T7-secretion, and SaPI5-excision.Scientific reports · 2019Article
- Regulation ofMicrobiology spectrum · 2019Review
- The ClpXP protease is dispensable for degradation of unfolded proteins in Staphylococcus aureus.Scientific reports · 2017Article
- Article
- Salmonella Typhimurium undergoes distinct genetic adaption during chronic infections of mice.BMC microbiology · 2016Article
- Norlichexanthone Reduces Virulence Gene Expression and Biofilm Formation in Staphylococcus aureus.PloS one · 2016Article
- Stepwise decrease in daptomycin susceptibility in clinical Staphylococcus aureus isolates associated with an initial mutation in rpoB and a compensatory inactivation of the clpX gene.Antimicrobial agents and chemotherapy · 2015Article
- Role of adaptor TrfA and ClpPC in controlling levels of SsrA-tagged proteins and antitoxins in Staphylococcus aureus.Journal of bacteriology · 2014Article
- β-Lactam resistance in methicillin-resistant Staphylococcus aureus USA300 is increased by inactivation of the ClpXP protease.Antimicrobial agents and chemotherapy · 2014Article
- Regulation of expression of abcA and its response to environmental conditions.Journal of bacteriology · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Clp ATPases (Hsp100) constitute a family of closely related proteins that have protein reactivating and remodelling activities typical of molecular chaperones. In Staphylococcus aureus the ClpX chaperone is essential for virulence and for transcription of spa encoding Protein A. The present study was undertaken to elucidate the mechanism by which ClpX stimulates expression of Protein A. For this purpose, we prepared antibodies directed against Rot, an activator of spa transcription, and demonstrated that cells devoid of ClpX contain three-fold less Rot than wild-type cells. By varying Rot expression from an inducible promoter we showed that expression of Protein A requires a threshold level of Rot. In the absence of ClpX the Rot content is reduced below this threshold level, hence, explaining the substantially reduced Protein A expression in the clpX mutant. Experiments addressed at pinpointing the role of ClpX in Rot synthesis revealed that ClpX is required for translation of Rot. Interestingly, translation of the spa mRNA was, like the rot mRNA, enhanced by ClpX. These data demonstrate that ClpX performs dual roles in regulating Protein A expression, as ClpX stimulates transcription of spa by enhancing translation of Rot, and that ClpX additionally is required for full translation of the spa mRNA. The current findings emphasize that ClpX has a central role in fine-tuning virulence regulation in S. aureus.
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Registered trials
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.