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Bacillithiol has a role in F e– S cluster biogenesis in S taphylococcus aureus
Author(s) -
RosarioCruz Zuelay,
Chahal Harsimranjit K.,
Mike Laura A.,
Skaar Eric P.,
Boyd Jeffrey M.
Publication year - 2015
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13115
Subject(s) - aconitase , biology , biogenesis , biochemistry , enzyme , metabolism , phenotype , amino acid , glutathione , isoleucine , leucine , genetics , gene
Summary S taphylococcus 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 .