ArticleMolecular microbiology2017
Bacillus subtilis MntR coordinates the transcriptional regulation of manganese uptake and efflux systems.
Article in Molecular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed.
- The phenotypic landscape of the model firmicuteProceedings of the National Academy of Sciences of the United States of America · 2026Article
- MntR Mediates LiaSR-RegulatedMicroorganisms · 2026Article
- MneA and TerC exhibit distinct roles in manganese detoxification and virulence inApplied and environmental microbiology · 2026Article
- MeeY and YybP, two proteins regulated by manganese-sensing riboswitches, are required for Bacillus subtilis biofilm formation.NPJ biofilms and microbiomes · 2026Article
- Operonic architecture of bacterial metal response: envelope constraints, evolutionary mobility, and bioremediation design rules.World journal of microbiology & biotechnology · 2026Review
- Article
- Fermentative growth decreases the iron demand of Staphylococcus aureus.Journal of inorganic biochemistry · 2026Article
- Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025Review
- Impact of energy metabolism pathways in promoting phytoremediation of cadmium contamination by Bacillus amyloliquefaciens Bam1.Bioresources and bioprocessing · 2025Article
- Reductive activation of the disulfide-containing antibiotic thiolutin is mediated by both bacillithiol and FAD-dependent disulfide reductases.Journal of bacteriology · 2025Article
- The TerC family metal chaperone MeeY enables surfactin export inJournal of bacteriology · 2025Article
- Structural basis for transcription activation through cooperative recruitment of MntR.Nature communications · 2025Article
- Metals in Motion: Understanding Labile Metal Pools in Bacteria.Biochemistry · 2025Review
- Metalation of Extracytoplasmic Proteins and Bacterial Cell Envelope Homeostasis.Annual review of microbiology · 2024Review
- Exploring the manganese-dependent interaction between a transcription factor and its corresponding DNA: insights from gas-phase electrophoresis on a nES GEMMA instrument.Analytical and bioanalytical chemistry · 2024Article
- Calcium RescuesMicroorganisms · 2024Article
- Advances in Research on Bacterial Oxidation of Mn(II): A Visualized Bibliometric Analysis Based on CiteSpace.Microorganisms · 2024Review
- TheJournal of bacteriology · 2024Article
- ThebioRxiv : the preprint server for biology · 2024Article
- Functional characterization of a TerC family protein ofApplied and environmental microbiology · 2024Article
10 more citing papers are in PubMed but not listed here.
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5 authors.
Funding
Abstract
The Bacillus subtilis MntR metalloregulatory protein senses manganese, an essential element required for central metabolism, oxidative stress resistance and replication. An mntR null mutant is highly sensitive to Mn(II) intoxication, which is attributed in part to the constitutive expression of two importers: the proton-dependent NRAMP family transporter MntH and the ABC transporter MntABCD. Here, we show that an mntR null mutant is still sensitive to Mn(II) intoxication even if both of the import systems are absent. This Mn(II) sensitivity results from the requirement for MntR to activate the transcription of two genes encoding cation diffusion facilitator (CDF) family efflux pumps. Physiological studies indicate that MneP (formerly YdfM) serves as the primary Mn(II) efflux pump with MneS (formerly YeaB) playing a secondary role. Mutant strains lacking mneP are Mn(II) sensitive and accumulate elevated levels of Mn(II), and these effects are exacerbated in a mneP mneS double mutant. DNA-binding and in vitro transcription studies demonstrate that MntR binds to both the mneP and mneS regulatory regions and directly activates transcription in response to levels of Mn(II) several-fold higher than required for repression of import genes. These results highlight the delicate balance of Mn(II) uptake and efflux systems controlled by MntR.
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