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Cited by 120Redox biology and oxidative stressBacterial Genetics and BiotechnologySulfur Compounds in Biology

The Role of Bacillithiol in Gram-Positive Firmicutes

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Chandrangsu, Pete, Loi, Vu Van, Antelmann, Haike, Helmann, John D.·2018·Antioxidants & Redox Signaling
DOI 10.1089/ars.2017.7057PMC PMC5790435
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Abstract

SIGNIFICANCE: Since the discovery and structural characterization of bacillithiol (BSH), the biochemical functions of BSH-biosynthesis enzymes (BshA/B/C) and BSH-dependent detoxification enzymes (FosB, Bst, GlxA/B) have been explored in Bacillus and Staphylococcus species. It was shown that BSH plays an important role in detoxification of reactive oxygen and electrophilic species, alkylating agents, toxins, and antibiotics. Recent Advances: More recently, new functions of BSH were discovered in metal homeostasis (Zn buffering, Fe-sulfur cluster, and copper homeostasis) and virulence control in Staphylococcus aureus. Unexpectedly, strains of the S. aureus NCTC8325 lineage were identified as natural BSH-deficient mutants. Modern mass spectrometry-based approaches have revealed the global reach of protein S-bacillithiolation in Firmicutes as an important regulatory redox modification under hypochlorite stress. S-bacillithiolation of OhrR, MetE, and glyceraldehyde-3-phosphate dehydrogenase (Gap) functions, analogous to S-glutathionylation, as both a redox-regulatory device and in thiol protection under oxidative stress. CRITICAL ISSUES: Although the functions of the bacilliredoxin (Brx) pathways in the reversal of S-bacillithiolations have been recently addressed, significantly more work is needed to establish the complete Brx reduction pathway, including the major enzyme(s), for reduction of oxidized BSH (BSSB) and the targets of Brx action in vivo. FUTURE DIRECTIONS: Despite the large number of identified S-bacillithiolated proteins, the physiological relevance of this redox modification was shown for only selected targets and should be a subject of future studies. In addition, many more BSH-dependent detoxification enzymes are evident from previous studies, although their roles and biochemical mechanisms require further study. This review of BSH research also pin-points these missing gaps for future research. Antioxid. Redox Signal. 28, 445-462.

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  • In B. subtilis, bacillithiol is important for the synthesis of FeS proteins.

    “In B. subtilis, bacillithiol (BSH)145 is important for the synthesis of FeS proteins.146,147”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [145]

    The “Iron-sulfur cluster assembly” section links bacillithiol to FeS biogenesis and reduced FeS-enzyme activity, but the evidence concerns S. aureus, not B. subtilis. The copy does not establish that bacillithiol is important for FeS-protein synthesis in B. subtilis. No page number is available in the indexed copy. (LLM, conf=0.88)

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Sorted by citations

Authors
Chandrangsu, P., Loi, V. V., Antelmann, H., & Helmann, J. D.
Affiliations
  • Cornell University (US)
  • Freie Universität Berlin (DE)
Corresponding author
  • Antelmann, Haike
  • Helmann, John D.
ORCID
Venue
Antioxidants & Redox Signaling
Publisher
SAGE Publications
Published
2018-02-20
Volume
28
Issue
6
Pages
445-462
ISSN
  • 1523-0864 (ISSN-L)
  • 1557-7716
DOI
10.1089/ars.2017.7057
PMC
PMC5790435
OpenAlex
W2597318279
Cited by
120
References
7
Citations by year
2026: 9 · 2025: 19 · 2024: 10 · 2023: 10 · 2022: 11 · 2021: 11 · 2020: 15 · 2019: 17 · 2018: 11 · 2017: 7
FWCI
1.32
Type
journal article
Language
en
Open access
Licence
www.liebertpub.com/nv/resources-tools/text-and-data-mining-policy/121/ (tdm)
Locations
  • Antioxidants and Redox Signaling (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • Refubium (Universitätsbibliothek der Freien Universität Berlin) (submittedVersion, cc-by-nc)
  • Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver
Funders
  • Deutsche Forschungsgemeinschaft (GRK1947, AN746/4‐1, GA 615585, AN746/3-1, SPP 1710)
  • National Institutes of Health
  • National Institute of General Medical Sciences (GM109993, GM059323, R01GM059323, R01GM109993, R35GM122461)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
Keywords
bacillithiol, redox regulation, detoxification enzymes, metal homeostasis, iron-sulfur clusters, copper homeostasis, Staphylococcus aureus, Bacillus, reactive oxygen species, alkylating agents, thiol protection, oxidative stress, S-glutathionylation
MeSH terms
Bacillota, Anti-Bacterial Agents, Bacillus subtilis, Cysteine, Glucosamine, Staphylococcus aureus, Sulfhydryl Compounds, Sulfur, Oxidative Stress

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