This Article Full Text Full Text (PDF) Supplemental material Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Smits, W. K. Articles by Kuipers, O. P. Search for Related Content PubMed PubMed Citation Articles by Smits, W. K. Articles by Kuipers, O. P.

Tricksy Business: Transcriptome Analysis Reveals the Involvement of Thioredoxin A in Redox Homeostasis, Oxidative Stress, Sulfur Metabolism, and Cellular Differentiation in Bacillus subtilis

Wiep Klaas Smits,¹ Jean-Yves F. Dubois,^2, Sierd Bron,¹ Jan Maarten van Dijl,^2, and Oscar P. Kuipers^1*

Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands,¹ Department of Pharmaceutical Biology, University of Groningen, A. Deusinglaan 1, 9713 AV, Groningen, The Netherlands²

Received 12 January 2005/ Accepted 10 March 2005

Thioredoxins are important thiol-reactive proteins. Most knowledge about this class of proteins is derived from proteome studies, and little is known about the global transcriptional response of cells to various thioredoxin levels. In Bacillus subtilis, thioredoxin A is encoded by trxA and is essential for viability. In this study, we report the effects of minimal induction of a strain carrying an IPTG (isopropyl-ß-D-thiogalactopyranoside)-inducible trxA gene (ItrxA) on transcription levels, as determined by DNA macroarrays. The effective depletion of thioredoxin A leads to the induction of genes involved in the oxidative stress response (but not those dependent on PerR), phage-related functions, and sulfur utilization. Also, several stationary-phase processes, such as sporulation and competence, are affected. The majority of these phenotypes are rescued by a higher induction level of ItrxA, leading to an approximately wild-type level of thioredoxin A protein. A comparison with other studies shows that the effects of thioredoxin depletion are distinct from, but show some similarity to, oxidative stress and disulfide stress. Some of the transcriptional effects may be linked to thioredoxin-interacting proteins. Finally, thioredoxin-linked processes appear to be conserved between prokaryotes and eukaryotes.

Supplemental material for this article may be found at http://jb.asm.org/.

Present address: Laboratory of Molecular Bacteriology, Department of Medical Microbiology, University Medical Center Groningen and University of Groningen, Hanzeplein 1, P.O. Box 30001, 9700 RB Groningen, The Netherlands.

This article has been cited by other articles:

• Moller, M. C., Hederstedt, L. (2008). Extracytoplasmic Processes Impaired by Inactivation of trxA (Thioredoxin Gene) in Bacillus subtilis. J. Bacteriol. 190: 4660-4665 [Abstract] [Full Text]  
• Choi, S.-Y., Reyes, D., Leelakriangsak, M., Zuber, P. (2006). The Global Regulator Spx Functions in the Control of Organosulfur Metabolism in Bacillus subtilis.. J. Bacteriol. 188: 5741-5751 [Abstract] [Full Text]  
• Zhang, X., Hu, Y., Guo, X., Lescop, E., Li, Y., Xia, B., Jin, C. (2006). The Bacillus subtilis YkuV Is a Thiol:Disulfide Oxidoreductase Revealed by Its Redox Structures and Activity. J. Biol. Chem. 281: 8296-8304 [Abstract] [Full Text]  
• Even, S., Burguiere, P., Auger, S., Soutourina, O., Danchin, A., Martin-Verstraete, I. (2006). Global Control of Cysteine Metabolism by CymR in Bacillus subtilis. J. Bacteriol. 188: 2184-2197 [Abstract] [Full Text]