ArticleJournal of bacteriology2015
The Staphylococcus aureus NuoL-like protein MpsA contributes to the generation of membrane potential.
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 29 papers.
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Who cites it
29 citing papers in PubMed, 44 citations in OpenAlex.
- mSphere Legacy: Fritz about Fritz.mSphere · 2026Article
- Structural basis of membrane potential coupled vectorial CO₂ hydration by the DAB2 complex in chemolithoautotrophs.Nature communications · 2026Article
- Formation of COBiofilm · 2025Article
- Bicarbonate Within: A Hidden Modulator of Antibiotic Susceptibility.Antibiotics (Basel, Switzerland) · 2025Review
- Article
- Role of the NaHCOMicrobiology spectrum · 2023Article
- Transcriptome analysis and prediction of the metabolic state of stress-induced viable but non-culturable Bacillus subtilis cells.Scientific reports · 2022Article
- Staphylococcus aureus Genomes Harbor Only MpsAB-Like Bicarbonate Transporter but Not Carbonic Anhydrase as Dissolved Inorganic Carbon Supply System.Microbiology spectrum · 2021Article
- The MpsB protein contributes to both the toxicity and immune evasion capacity ofMicrobiology (Reading, England) · 2021Article
- The MpsAB Bicarbonate Transporter Is Superior to Carbonic Anhydrase in Biofilm-Forming Bacteria with Limited COMicrobiology spectrum · 2021Article
- TheFrontiers in microbiology · 2021Article
- The alarmone (p)ppGpp confers tolerance to oxidative stress during the stationary phase by maintenance of redox and iron homeostasis in Staphylococcus aureus.Free radical biology & medicine · 2020Article
- Role of respiratory NADH oxidation in the regulation of Staphylococcus aureus virulence.EMBO reports · 2020Article
- High-throughput transposon sequencing highlights the cell wall as an important barrier for osmotic stress in methicillin resistant Staphylococcus aureus and underlines a tailored response to different osmotic stressors.Molecular microbiology · 2020Article
- Bactericidal Activity of the Bacterial ATP Synthase Inhibitor Tomatidine and the Combination of Tomatidine and Aminoglycoside Against Persistent and Virulent Forms ofFrontiers in microbiology · 2020Article
- The MarR-Type Repressor MhqR Confers Quinone and Antimicrobial Resistance inAntioxidants & redox signaling · 2019Article
- Proteomic and Membrane Lipid Correlates of Reduced Host Defense Peptide.Antibiotics (Basel, Switzerland) · 2019Article
- MpsAB is important for Staphylococcus aureus virulence and growth at atmospheric CONature communications · 2019Article
- Respiration and Small Colony Variants ofMicrobiology spectrum · 2019Review
- Artificial Selection for Pathogenicity Mutations inInfection and immunity · 2019Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In aerobic microorganisms, the entry point of respiratory electron transfer is represented by the NADH:quinone oxidoreductase. The enzyme couples the oxidation of NADH with the reduction of quinone. In the type 1 NADH:quinone oxidoreductase (Ndh1), this reaction is accompanied by the translocation of cations, such as H(+) or Na(+). In Escherichia coli, cation translocation is accomplished by the subunit NuoL, thus generating membrane potential (Δψ). Some microorganisms achieve NADH oxidation by the alternative, nonelectrogenic type 2 NADH:quinone oxidoreductase (Ndh2), which is not cation translocating. Since these enzymes had not been described in Staphylococcus aureus, the goal of this study was to identify proteins operating in the NADH:quinone segment of its respiratory chain. We demonstrated that Ndh2 represents a NADH:quinone oxidoreductase in S. aureus. Additionally, we identified a hypothetical protein in S. aureus showing sequence similarity to the proton-translocating subunit NuoL of complex I in E. coli: the NuoL-like protein MpsA. Mutants with deletion of the nuoL-like gene mpsA and its corresponding operon, mpsABC (mps for membrane potential-generating system), exhibited a small-colony-variant-like phenotype and were severely affected in Δψ and oxygen consumption rates. The MpsABC proteins did not confer NADH oxidation activity. Using an Na(+)/H(+) antiporter-deficient E. coli strain, we could show that MpsABC constitute a cation-translocating system capable of Na(+) transport. Our study demonstrates that MpsABC represent an important functional system of the respiratory chain of S. aureus that acts as an electrogenic unit responsible for the generation of Δψ.
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