ArticleMolecular microbiology2014
Bacillithiol is a major buffer of the labile zinc pool in Bacillus subtilis.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 96 citations in OpenAlex.
- Article
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- Reductive activation of the disulfide-containing antibiotic thiolutin is mediated by both bacillithiol and FAD-dependent disulfide reductases.Journal of bacteriology · 2025Article
- Bacteria Under Metal Stress-Molecular Mechanisms of Metal Tolerance.International journal of molecular sciences · 2025Review
- Metals in Motion: Understanding Labile Metal Pools in Bacteria.Biochemistry · 2025Review
- A metal-trap tests and refines blueprints to engineer cellular protein metalation with different elements.Nature communications · 2025Article
- Anaerobic HgII reduction is driven by cellular HgII-thiol interactions.Access microbiology · 2025Article
- From the outer space to the inner cell: deconvoluting the complexity ofMicrobiology spectrum · 2024Article
- Sulfinamide Formation from the Reaction of Bacillithiol and Nitroxyl.ACS chemical biology · 2023Article
- Protein metalation in a nutshell.FEBS letters · 2023Review
- Poly-Gamma-Glutamic Acid Secretion Protects Bacillus subtilis from Zinc and Copper Intoxication.Microbiology spectrum · 2022Article
- Protein metalation in biology.Current opinion in chemical biology · 2022Review
- Direct Detection of the Labile Nickel Pool inJournal of the American Chemical Society · 2021Article
- Low-molecular-mass labile metal pools in Escherichia coli: advances using chromatography and mass spectrometry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr (YpdA) disulfide reductase reduce S-bacillithiolated proteins.Redox biology · 2021Article
- Redox signaling through zinc activates the radiation response in Deinococcus bacteria.Scientific reports · 2021Article
- Article
- Chromatographic detection of low-molecular-mass metal complexes in the cytosol of Saccharomyces cerevisiae.Metallomics : integrated biometal science · 2020Article
- One-carbon metabolism, folate, zinc and translation.Microbial biotechnology · 2020Article
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6 authors at 1 institution in 2 countries.
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Abstract
Intracellular zinc levels are tightly regulated since zinc is an essential cofactor for numerous enzymes, yet can be toxic when present in excess. The majority of intracellular zinc is tightly associated with proteins and is incorporated during synthesis from a poorly defined pool of kinetically labile zinc. In Bacillus subtilis, this labile pool is sensed by equilibration with the metalloregulator Zur, as an indication of zinc sufficiency, and by CzrA, as an indication of zinc excess. Here, we demonstrate that the low-molecular-weight thiol bacillithiol (BSH) serves as a major buffer of the labile zinc pool. Upon shift to conditions of zinc excess, cells transiently accumulate zinc in a low-molecular-weight pool, and this accumulation is largely dependent on BSH. Cells lacking BSH are more sensitive to zinc stress, and they induce zinc efflux at lower external zinc concentrations. Thiol reactive agents such as diamide and cadmium induce zinc efflux by interfering with the Zn-buffering function of BSH. Our data provide new insights into intracellular zinc buffering and may have broad relevance given the presence of BSH in pathogens and the proposed role of zinc sequestration in innate immunity.
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