期刊
JOURNAL OF BACTERIOLOGY
卷 191, 期 24, 页码 7520-7530出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00937-09
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资金
- Deutsche Forschungsgemeinschaft [AN 746/2-1, SFB/TRR34/1-2006]
- Bundesministerium fur Bildung und Forschung [BACELL-SysMo 031397A]
- Bildungsministerium of the State Mecklenburg-Vorpommern
- European Union [LSHG-CT-2004-503468]
- BACELL-BaSysBio [LSHG-CT-2006-037469]
Glutathione constitutes a key player in the thiol redox buffer in many organisms. However, the gram-positive bacteria Bacillus subtilis and Staphylococcus aureus lack this low-molecular-weight thiol. Recently, we identified S-cysteinylated proteins in B. subtilis after treatment of cells with the disulfide-generating electrophile diamide. S cysteinylation is thought to protect protein thiols against irreversible oxidation to sulfinic and sulfonic acids. Here we show that S thiolation occurs also in S. aureus proteins after exposure to diamide. We further analyzed the formation of inter-and intramolecular disulfide bonds in cytoplasmic proteins using diagonal nonreducing/reducing sodium dodecyl sulfate gel electrophoresis. However, only a few proteins were identified that form inter-or intramolecular disulfide bonds under control and diamide stress conditions in B. subtilis and S. aureus. Depletion of the cysteine pool was concomitantly measured in B. subtilis using a metabolomics approach. Thus, the majority of reversible thiol modifications that were previously detected by two-dimensional gel fluorescence-based thiol modification assay are most likely based on S thiolations. Finally, we found that a glutathione-producing B. subtilis strain which expresses the Listeria monocytogenes gshF gene did not show enhanced oxidative stress resistance compared to the wild type.
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