ArticleScientific reports2017
Rewiring of the FtsH regulatory network by a single nucleotide change in saeS of Staphylococcus aureus.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Pyrimidine sufficiency is required for Sae two-component system signaling inJournal of bacteriology · 2025Article
- Novel antibiotics againstMedComm · 2025Article
- Glycine betaine metabolism is enabled inApplied and environmental microbiology · 2024Article
- Article
- Molybdopterin biosynthesis pathway contributes to the regulation of SaeRS two-component system by ClpP inVirulence · 2022Article
- Convergent Evolution of Antibiotic Tolerance in Patients with Persistent Methicillin-Resistant Staphylococcus aureus Bacteremia.Infection and immunity · 2022Article
- Ftsh Sensitizes Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2021Article
- Integrated Proteomic and Transcriptomic Analyses Reveal the Roles ofFrontiers in microbiology · 2021Article
- A Membrane-Bound Transcription Factor is Proteolytically Regulated by the AAA+ Protease FtsH in Staphylococcus aureus.Journal of bacteriology · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
In the Gram-positive pathogen Staphylococcus aureus, the membrane-bound ATP-dependent metalloprotease FtsH plays a critical role in resistance to various stressors. However, the molecular mechanism of the FtsH functions is not known. Here, we identified core FtsH target proteins in S. aureus. In the strains Newman and USA300, the abundance of 33 proteins were altered in both strains, of which 11 were identified as core FtsH substrate protein candidates. In the strain Newman and some other S. aureus strains, the sensor histidine kinase SaeS has an L18P (T53C in saeS) substitution, which transformed the protein into an FtsH substrate. Due to the increase of SaeS L18P in the ftsH mutant, Eap, a sae-regulon protein, was also increased in abundance, causing the Newman-specific cell-aggregation phenotype. Regardless of the strain background, however, the ftsH mutants showed lower virulence and survival in a murine infection model. Our study illustrates the elasticity of the bacterial regulatory network, which can be rewired by a single substitution mutation.
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