Analysis of mutants disrupted in bacillithiol metabolism in Staphylococcus aureus

•S. aureus bacillithiol mutants are sensitive to oxidative, alkylating and metal stress.•BSH deacetylase is a dual function enzyme, acting also as a BSH conjugate amidase.•S. aureus USA 300 LAC 2626 encodes a bacillithiol-S-transferase. Bacillithiol (BSH), an α-anomeric glycoside of l-cysteinyl-d-gl...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2013-06, Vol.436 (2), p.128-133
Main Authors: Rajkarnikar, Arishma, Strankman, Andrew, Duran, Shayla, Vargas, Derek, Roberts, Alexandra A., Barretto, Kathryn, Upton, Heather, Hamilton, Christopher J., Rawat, Mamta
Format: Article
Language:English
Subjects:
Bacillithiol
Bacillithiol conjugate amidase
Bacillthiol-S-transferase
Bacillus subtilis
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Biosynthetic Pathways - genetics
Chromatography, High Pressure Liquid
Cysteine - analogs & derivatives
Cysteine - metabolism
Glucosamine - analogs & derivatives
Glucosamine - metabolism
Iodoacetamide - pharmacology
Metals - pharmacology
Microbial Viability - drug effects
Microbial Viability - genetics
Mutation
Oxidants - pharmacology
Pyruvaldehyde - pharmacology
Staphylococcus aureus
Staphylococcus aureus - enzymology
Staphylococcus aureus - genetics
Staphylococcus aureus - metabolism
Sulfhydryl Compounds - metabolism
Thiols
Time Factors
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Summary:•S. aureus bacillithiol mutants are sensitive to oxidative, alkylating and metal stress.•BSH deacetylase is a dual function enzyme, acting also as a BSH conjugate amidase.•S. aureus USA 300 LAC 2626 encodes a bacillithiol-S-transferase. Bacillithiol (BSH), an α-anomeric glycoside of l-cysteinyl-d-glucosaminyl-l-malate, is a major low molecular weight thiol found in low GC Gram-positive bacteria, such as Staphylococcus aureus. Like other low molecular weight thiols, BSH is likely involved in protection against a number of stresses. We examined S. aureus transposon mutants disrupted in each of the three genes associated with BSH biosynthesis. These mutants are sensitive to alkylating stress, oxidative stress, and metal stress indicating that BSH and BSH-dependent enzymes are involved in protection of S. aureus. We further demonstrate that BshB, a deacetylase involved in the second step of BSH biosynthesis, also acts as a BSH conjugate amidase and identify S. aureus USA 300 LAC 2626 as a BSH-S-transferase, which is able to conjugate chlorodinitrobenzene, cerulenin, and rifamycin to BSH.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2013.04.027