Staphylococcus aureus DsbA is a membrane-bound lipoprotein with thiol-disulfide oxidoreductase activity

DsbA proteins, the primary catalysts of protein disulfide bond formation, are known to affect virulence and penicillin resistance in Gram-negative bacteria. We identified a putative DsbA homologue in the Gram-positive pathogen Staphylococcus aureus that was able to restore the motility phenotype of...

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Bibliographic Details
Published in:Archives of microbiology 2005-11, Vol.184 (2), p.117-128
Main Authors: DUMOULIN, Alexis, GRAUSCHOPF, Ulla, BISCHOFF, Markus, THÖNY-MEYER, Linda, BERGER-BÄCHI, Brigitte
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Bacteria
Bacteriology
Base Sequence
Biological and medical sciences
Caenorhabditis elegans
Chemical bonds
E coli
Escherichia coli
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
Genetic Complementation Test
Genetics
Metabolism. Enzymes
Mice
Microbiology
Molecular Sequence Data
Protein Disulfide Reductase (Glutathione) - metabolism
Protein Disulfide-Isomerases - metabolism
Redox potential
Sequence Alignment
Staphylococcus aureus
Staphylococcus aureus - enzymology
Staphylococcus aureus - genetics
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Summary:DsbA proteins, the primary catalysts of protein disulfide bond formation, are known to affect virulence and penicillin resistance in Gram-negative bacteria. We identified a putative DsbA homologue in the Gram-positive pathogen Staphylococcus aureus that was able to restore the motility phenotype of an Escherichia coli dsbA mutant and thus demonstrated a functional thiol oxidoreductase activity. The staphylococcal DsbA (SaDsbA) had a strong oxidative redox potential of -131 mV. The persistence of the protein throughout the growth cycle despite its predominant transcription during exponential growth phase suggested a rather long half-life for the SaDsbA. SaDsbA was found to be a membrane localised lipoprotein, supporting a role in disulfide bond formation. But so far, neither in vitro nor in vivo phenotype could be identified in a staphylococcal dsbA mutant, leaving its physiological role unknown. The inability of SaDsbA to interact with the E. coli DsbB and the lack of an apparent staphylococcal DsbB homologue suggest an alternative re-oxidation pathway for the SaDsbA.
ISSN:0302-8933
1432-072X
DOI:10.1007/s00203-005-0024-1