This Article Full Text Full Text (PDF) 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 Sala, C. Articles by Ghisotti, D. Search for Related Content PubMed PubMed Citation Articles by Sala, C. Articles by Ghisotti, D.

Mycobacterium tuberculosis FurA Autoregulates Its Own Expression

Dipartimento di Genetica e di Biologia dei Microrganismi, Università di Milano, Milan,¹ Dipartimento di Genetica e di Microbiologia A. Buzzati Traverso, Università di Pavia, Pavia, Italy²

Received 11 April 2003/ Accepted 25 June 2003

The furA-katG region of Mycobacterium tuberculosis, encoding a Fur-like protein and the catalase-peroxidase, is highly conserved among mycobacteria. Both genes are induced upon oxidative stress. In this work we analyzed the M. tuberculosis furA promoter region. DNA fragments were cloned upstream of the luciferase reporter gene, and promoter activity in Mycobacterium smegmatis was measured in both the presence and absence of oxidative stress. The shortest fragment containing an inducible promoter extends 45 bp upstream of furA. In this region, -35 and -10 promoter consensus sequences can be identified, as well as a 23-bp AT-rich sequence that is conserved in the nonpathogenic but closely related M. smegmatis. M. tuberculosis FurA was purified and found to bind upstream of furA by gel shift analysis. A ca. 30-bp DNA sequence, centered on the AT-rich region, was essential for FurA binding and protected by FurA in footprinting analysis. Peroxide treatment of FurA abolished DNA binding. Three different AT-rich sequences mutagenized by site-directed mutagenesis were constructed. In each mutant, both M. tuberculosis FurA binding in vitro and pfurA regulation upon oxidative-stress in M. smegmatis were abolished. Thus, pfurA is an oxidative stress-responsive promoter controlled by the FurA protein.

This article has been cited by other articles:

• Ward, S. K., Hoye, E. A., Talaat, A. M. (2008). The Global Responses of Mycobacterium tuberculosis to Physiological Levels of Copper. J. Bacteriol. 190: 2939-2946 [Abstract] [Full Text]  
• Boulette, M. L., Payne, S. M. (2007). Anaerobic Regulation of Shigella flexneri Virulence: ArcA Regulates fur and Iron Acquisition Genes. J. Bacteriol. 189: 6957-6967 [Abstract] [Full Text]  
• Lee, H.-J., Bang, S. H., Lee, K.-H., Park, S.-J. (2007). Positive Regulation of fur Gene Expression via Direct Interaction of Fur in a Pathogenic Bacterium, Vibrio vulnificus. J. Bacteriol. 189: 2629-2636 [Abstract] [Full Text]  
• Bagchi, G., Chauhan, S., Sharma, D., Tyagi, J. S. (2005). Transcription and autoregulation of the Rv3134c-devR-devS operon of Mycobacterium tuberculosis. Microbiology 151: 4045-4053 [Abstract] [Full Text]  
• Canneva, F., Branzoni, M., Riccardi, G., Provvedi, R., Milano, A. (2005). Rv2358 and FurB: Two Transcriptional Regulators from Mycobacterium tuberculosis Which Respond to Zinc. J. Bacteriol. 187: 5837-5840 [Abstract] [Full Text]  
• Ramos, J. L., Martinez-Bueno, M., Molina-Henares, A. J., Teran, W., Watanabe, K., Zhang, X., Gallegos, M. T., Brennan, R., Tobes, R. (2005). The TetR Family of Transcriptional Repressors. Microbiol. Mol. Biol. Rev. 69: 326-356 [Abstract] [Full Text]  
• Katona, L. I., Tokarz, R., Kuhlow, C. J., Benach, J., Benach, J. L. (2004). The Fur Homologue in Borrelia burgdorferi. J. Bacteriol. 186: 6443-6456 [Abstract] [Full Text]