| pubmed-article:19837798 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19837798 | lifeskim:mentions | umls-concept:C0004595 | lld:lifeskim |
| pubmed-article:19837798 | lifeskim:mentions | umls-concept:C0038172 | lld:lifeskim |
| pubmed-article:19837798 | lifeskim:mentions | umls-concept:C0521449 | lld:lifeskim |
| pubmed-article:19837798 | lifeskim:mentions | umls-concept:C0751973 | lld:lifeskim |
| pubmed-article:19837798 | lifeskim:mentions | umls-concept:C1444748 | lld:lifeskim |
| pubmed-article:19837798 | lifeskim:mentions | umls-concept:C0011953 | lld:lifeskim |
| pubmed-article:19837798 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:19837798 | pubmed:dateCreated | 2009-11-25 | lld:pubmed |
| pubmed-article:19837798 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:19837798 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19837798 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19837798 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19837798 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19837798 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19837798 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:19837798 | pubmed:issn | 1098-5530 | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:HeckerMichael... | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:CohenGeraldG | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:BorovokIlyaI | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:AharonowitzYa... | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:BecherDörteD | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:AntelmannHaik... | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:LindequistUlr... | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:HochgräfeFalk... | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:LalkMichaelM | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:LiebekeManuel... | lld:pubmed |
| pubmed-article:19837798 | pubmed:author | pubmed-author:PötherDierk-C... | lld:pubmed |
| pubmed-article:19837798 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19837798 | pubmed:volume | 191 | lld:pubmed |
| pubmed-article:19837798 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19837798 | pubmed:authorsComplete | Y | lld:pubmed |
