Diamide triggers mainly S Thiolations in the cytoplasmic proteomes of Bacillus subtilis and Staphylococcus aureus

Abstract:

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.

SEEK ID: https://fairdomhub.org/publications/80

PubMed ID: 19837798

Projects: BaCell-SysMO

Journal: J. Bacteriol.

Citation:

Date Published: 16th Oct 2009

Authors: Dierk-Christoph Pöther, Manuel Liebeke, Falko Hochgräfe, Haike Antelmann, Dörte Becher, Michael Lalk, Ulrike Lindequist, Ilya Borovok, Gerald Cohen, Yair Aharonowitz, Michael Hecker

Help
help Creator
Activity

Views: 2492

Created: 20th Aug 2010 at 16:01

Last updated: 5th Oct 2010 at 09:31

help Attributions

None

Related items

Powered by
Seek new full
(v.1.8.2)
Copyright © 2008 - 2019 The University of Manchester and HITS gGmbH