Bacillithiol: a key protective thiol in<i>Staphylococcus</i><i>aureus</i>

Perera, Varahenage R.; Newton, Gerald L.; Pogliano, Kit

doi:10.1586/14787210.2015.1064309

Cited by 43 publications

(49 citation statements)

References 95 publications

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“…These thiol-redox systems have largely overlapping functions, and therefore, loss of one or even both of them is not unprecedented [120,122]. Alternative antioxidant systems are also described and can be exemplified by the ones based on mycothiol or bacilithiol in various bacteria, phytochelatins in plants, and ovothiol in sea urchins [123][124][125][126]. Trypanosomatids are known to have developed a minimalistic thiol-redox system based solely on trypanothione [40,127,128].…”

Section: Nadph-dependent Thiol-redox Systemsmentioning

confidence: 99%

Evolution of metabolic capabilities and molecular features of diplonemids, kinetoplastids, and euglenids

et al. 2020

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Background: The Euglenozoa are a protist group with an especially rich history of evolutionary diversity. They include diplonemids, representing arguably the most species-rich clade of marine planktonic eukaryotes; trypanosomatids, which are notorious parasites of medical and veterinary importance; and free-living euglenids. These different lifestyles, and particularly the transition from free-living to parasitic, likely require different metabolic capabilities. We carried out a comparative genomic analysis across euglenozoan diversity to see how changing repertoires of enzymes and structural features correspond to major changes in lifestyles. Results: We find a gradual loss of genes encoding enzymes in the evolution of kinetoplastids, rather than a sudden decrease in metabolic capabilities corresponding to the origin of parasitism, while diplonemids and euglenids maintain more metabolic versatility. Distinctive characteristics of molecular machines such as kinetochores and the pre-replication complex that were previously considered specific to parasitic kinetoplastids were also identified in their free-living relatives. Therefore, we argue that they represent an ancestral rather than a derived state, as thought until the present. We also found evidence of ancient redundancy in systems such as NADPH-dependent thiol-redox. Only the genus Euglena possesses the combination of trypanothione-, glutathione-, and thioredoxin-based systems supposedly present in the euglenozoan common ancestor, while other representatives of the phylum have lost one or two of these systems. Lastly, we identified convergent losses of specific metabolic capabilities between free-living kinetoplastids and ciliates. Although this observation requires further examination, it suggests that certain eukaryotic lineages are predisposed to such convergent losses of key enzymes or whole pathways. Conclusions: The loss of metabolic capabilities might not be associated with the switch to parasitic lifestyle in kinetoplastids, and the presence of a highly divergent (or unconventional) kinetochore machinery might not be restricted to this protist group. The data derived from the transcriptomes of free-living early branching prokinetoplastids suggests that the pre-replication complex of Trypanosomatidae is a highly divergent version of the conventional machinery. Our findings shed light on trends in the evolution of metabolism in protists in general and open multiple avenues for future research.

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Section: Nadph-dependent Thiol-redox Systemsmentioning

confidence: 99%

Evolution of metabolic capabilities and molecular features of diplonemids, kinetoplastids, and euglenids

et al. 2020

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“…However, to our knowledge there have been no reports on the impact of diallylpolysulfanes on intracellular depletion of individual low molecular weight thiols or the intracellular production of allyl thiol/persulfides. Instead of GSH, many Gram positive bacteria produce alternative, functionally equivalent, low molecular weight thiols such as mycothiol (actinomycetes) [18,19] and bacillithiol (BSH) (firmicutes) [20,21,22]. Using Bacillus subtilis as a model BSH-utilising bacteria, we compare the antimicrobial activities of DAS1 to DAS6.…”

Section: Introduction1mentioning

confidence: 99%

Antimicrobial garlic-derived diallyl polysulfanes: Interactions with biological thiols in Bacillus subtilis

Arbach

Santana

Moxham

et al. 2019

Biochimica et Biophysica Acta (BBA) - General Subjects

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Background: Diallylpolysulfanes are the key constituents of garlic oils, known to exhibit broad spectrum anticancer and antimicrobial activity. Studies in vitro, and in mammalian cells, have shown they react, via thiolpolysulfane exchange, with their major low molecular weight thiol, glutathione. However, there are no detailed reports of diallylpolysulfane effects on other common thiol metabolites (cysteine and coenzyme A) or major thiol cofactors (e.g. bacillithiol) that many Gram positive bacteria produce instead of glutathione. Methods: Diallylpolysulfanes were individually purified then screened for antimicrobial activity against Bacillus subtilis. Their impact on thiol metabolites (bacillithiol, cysteine, coenzyme A, protein thiols allyl thiols//persulfides) in B. subtilis cultures were analysed, by HPLC. Results: Diallylpolysulfane bioactivity increased with increasing chain length up to diallyltetrasulfane, but then plateaued. Within two minutes of treating B. subtilis with diallyltrisulfane or diallyltetrasulfane intracellular bacillithiol levels decreased by ~90%. Cysteine and CoA were also affected but to a lesser degree. This was accompanied by the accumulation of allyl thiol and allyl persulfide. A significant level of proteinS -allylation was also detected. Conclusions: In addition to the major low molecular weight thiol, diallylpolysulfanes can also have an impact on other thiol metabolites and protein thiols. General Significance: This study shows the rapid parallel impact of polysulfanes on different biological thiols inside Bacillus subtilis alongside the concomitant generation of allyl thiols and persulfides.

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“…The S-thioallylated di-and trisulfanes were the major GSH conjugates measured upon GSH exposure to DAS3-6 in vitro [9]. In contrast to E. coli and eukaryotes, the Gram-positive bacterium B. subtilis does not utilize GSH, but instead produces bacillithiol (BSH) as alternative LMW thiol [21][22][23]. In B. subtilis, the depletion of the BSH and cysteine by the polysulfanes DAS3-4 occurred rapidly and was accompanied by formation of allyl thiols as polysulfane detoxification products [9].…”

Section: Introductionmentioning

confidence: 99%

The Disulfide Stress Response and Protein S-thioallylation Caused by Allicin and Diallyl Polysulfanes in Bacillus subtilis as Revealed by Transcriptomics and Proteomics

et al. 2019

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Garlic plants (Allium sativum L.) produce antimicrobial compounds, such as diallyl thiosulfinate (allicin) and diallyl polysulfanes. Here, we investigated the transcriptome and protein S-thioallylomes under allicin and diallyl tetrasulfane (DAS4) exposure in the Gram-positive bacterium Bacillus subtilis. Allicin and DAS4 caused a similar thiol-specific oxidative stress response, protein and DNA damage as revealed by the induction of the OhrR, PerR, Spx, YodB, CatR, HypR, AdhR, HxlR, LexA, CymR, CtsR, and HrcA regulons in the transcriptome. At the proteome level, we identified, in total, 108 S-thioallylated proteins under allicin and/or DAS4 stress. The S-thioallylome includes enzymes involved in the biosynthesis of surfactin (SrfAA, SrfAB), amino acids (SerA, MetE, YxjG, YitJ, CysJ, GlnA, YwaA), nucleotides (PurB, PurC, PyrAB, GuaB), translation factors (EF-Tu, EF-Ts, EF-G), antioxidant enzymes (AhpC, MsrB), as well as redox-sensitive MarR/OhrR and DUF24-family regulators (OhrR, HypR, YodB, CatR). Growth phenotype analysis revealed that the low molecular weight thiol bacillithiol, as well as the OhrR, Spx, and HypR regulons, confer protection against allicin and DAS4 stress. Altogether, we show here that allicin and DAS4 cause a strong oxidative, disulfide and sulfur stress response in the transcriptome and widespread S-thioallylation of redox-sensitive proteins in B. subtilis. The results further reveal that allicin and polysulfanes have similar modes of actions and thiol-reactivities and modify a similar set of redox-sensitive proteins by S-thioallylation.

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Bacillithiol: a key protective thiol inStaphylococcusaureus

Cited by 43 publications

References 95 publications

Evolution of metabolic capabilities and molecular features of diplonemids, kinetoplastids, and euglenids

Evolution of metabolic capabilities and molecular features of diplonemids, kinetoplastids, and euglenids

Antimicrobial garlic-derived diallyl polysulfanes: Interactions with biological thiols in Bacillus subtilis

The Disulfide Stress Response and Protein S-thioallylation Caused by Allicin and Diallyl Polysulfanes in Bacillus subtilis as Revealed by Transcriptomics and Proteomics

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