Cited by 50Metalloenzymes and iron-sulfur proteinsSulfur Compounds in BiologyBacterial Genetics and Biotechnology

Bacillithiol has a role in F e–S cluster biogenesis in Staphylococcus aureus

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Rosario‐Cruz, Zuelay, Chahal, Harsimranjit K., Mike, Laura A., Skaar, Eric P., Boyd, Jeffrey M.·2015·Molecular Microbiology

Abstract

Summary: Staphylococcus aureus does not produce the low‐molecular‐weight (LMW) thiol glutathione, but it does produce the LMW thiol bacillithiol (BSH). To better understand the roles that BSH plays in staphylococcal metabolism, we constructed and examined strains lacking BSH. Phenotypic analysis found that the BSH‐deficient strains cultured either aerobically or anaerobically had growth defects that were alleviated by the addition of exogenous iron (F e) or the amino acids leucine and isoleucine. The activities of the iron–sulfur (F e–S) cluster‐dependent enzymes LeuCD and IlvD, which are required for the biosynthesis of leucine and isoleucine, were decreased in strains lacking BSH. The BSH‐deficient cells also had decreased aconitase and glutamate synthase activities, suggesting a general defect in F e–S cluster biogenesis. The phenotypes of the BSH‐deficient strains were exacerbated in strains lacking the F e–S cluster carrier Nfu and partially suppressed by multicopy expression of either sufA or nfu, suggesting functional overlap between BSH and F e–S carrier proteins. Biochemical analysis found that SufA bound and transferred F e–S clusters to apo‐aconitase, verifying that it serves as an F e–S cluster carrier. The results presented are consistent with the hypothesis that BSH has roles in F e homeostasis and the carriage of F e–S clusters to apo‐proteins in S. aureus.

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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 [147]

    The Abstract reports that bacillithiol-deficient S. aureus has reduced activity of Fe–S-dependent enzymes, supporting a role for bacillithiol in Fe–S cluster biogenesis in that species. The Discussion says future studies are needed to determine whether this role is conserved in other bacillithiol-producing species; it does not establish the claim for B. subtilis. Page numbers are unavailable in our copy. (LLM, conf=0.88)

    Experimental — accuracy not yet measured
  • LMW thiols GSH and BSH are implicated in assembly of FeS clusters.

    “and in assembly of FeS clusters.147,212”

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Authors
Rosario‐Cruz, Z., Chahal, H. K., Mike, L. A., Skaar, E. P., & Boyd, J. M.
Affiliations
  • Rutgers, The State University of New Jersey (US)
  • Vanderbilt University (US)
Corresponding author
Boyd, Jeffrey M.
Venue
Molecular Microbiology
Publisher
Wiley
Published
2015-07-30
Volume
98
Issue
2
Pages
218-242
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
OpenAlex
W2135763006
Cited by
50
References
8
Citations by year
2026: 2 · 2025: 5 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 5 · 2020: 6 · 2019: 7 · 2018: 6 · 2017: 5 · 2016: 6 · 2015: 1
FWCI
1.67
Type
journal article
Language
en
Open access
Locations
  • Molecular Microbiology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • Rutgers University Community Repository (Rutgers University) (submittedVersion)
Funders
  • Rutgers University
  • Charles and Johanna Busch Foundation
  • USDA MRF (NE−1028)
  • NIH (AI069233)
Topics
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
bacillithiol, iron-sulfur cluster assembly, Staphylococcus aureus, iron homeostasis, SufA, aconitase, glutamate synthase, leucine biosynthesis, isoleucine biosynthesis, low molecular weight thiols, iron deficiency
MeSH terms
Aconitate Hydratase, Apoproteins, Bacterial Proteins, Cysteine, Glucosamine, Glutamate Synthase, Homeostasis, Iron, Iron-Sulfur Proteins, Oxidation-Reduction, Phenotype, Staphylococcus aureus, Sulfur

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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