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Microbiology 153 (2007), 1081-1086; DOI  10.1099/mic.0.2006/004143-0
© 2007 Society for General Microbiology

The periplasmic thioredoxin SoxS plays a key role in activation in vivo of chemotrophic sulfur oxidation of Paracoccus pantotrophus

Grazyna Orawski, Frank Bardischewsky, Armin Quentmeier, Dagmar Rother and Cornelius G. Friedrich

Lehrstuhl für Technische Mikrobiologie, Fachbereich Bio- und Chemieingenieurwesen, Universität Dortmund, Emil-Figge-Strasse 66, D-44221 Dortmund, Germany

Correspondence
Cornelius G. Friedrich
cornelius.friedrich{at}udo.edu

The significance of the soxS gene product on chemotrophic sulfur oxidation of Paracoccus pantotrophus was investigated. The thioredoxin SoxS was purified, and the N-terminal amino acid sequence identified SoxS as the soxS gene product. The wild-type formed thiosulfate-oxidizing activity and Sox proteins during mixotrophic growth with succinate plus thiosulfate, while there was no activity, and only traces of Sox proteins, under heterotrophic conditions. The homogenote mutant strain GB{Omega}S is unable to express the soxSR genes, of which soxR encodes a transcriptional regulator. Strain GB{Omega}S cultivated mixotrophically showed about 22 % of the specific thiosulfate-dependent O2 uptake rate of the wild-type, and when cultivated heterotrophically it produced 35 % activity. However, under both mixotrophic and heterotrophic conditions, strain GB{Omega}S formed Sox proteins essential for sulfur oxidation in vitro at the same high level as the wild-type produced them during mixotrophic growth. Genetic complementation of strain GB{Omega}S with soxS restored the activity upon mixotrophic and heterotrophic growth. Chemical complementation by reductants such as L-cysteine, DTT and tris(2-carboxyethyl)phosphine also restored the activity of strain GB{Omega}S in the presence of chloramphenicol, which is an inhibitor of de novo protein synthesis. The data demonstrate that SoxS plays a key role in activation of the Sox enzyme system, and this suggests that SoxS is part of a novel type of redox control in P. pantotrophus.


Abbreviations: TCEP, tris(2-carboxyethyl)phosphine




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D. Rother, J. Ringk, and C. G. Friedrich
Sulfur oxidation of Paracoccus pantotrophus: the sulfur-binding protein SoxYZ is the target of the periplasmic thiol-disulfide oxidoreductase SoxS
Microbiology, July 1, 2008; 154(7): 1980 - 1988.
[Abstract] [Full Text] [PDF]




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