This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yamamoto, Y.
Right arrow Articles by Kamio, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yamamoto, Y.
Right arrow Articles by Kamio, Y.

 Previous Article  |  Next Article 

Journal of Bacteriology, July 2000, p. 3740-3747, Vol. 182, No. 13
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Role of the dpr Product in Oxygen Tolerance in Streptococcus mutans

Yuji Yamamoto,1 Masako Higuchi,1 Leslie B. Poole,2 and Yoshiyuki Kamio1,*

Laboratory of Applied Microbiology, Department of Molecular and Cell Biology, Graduate School of Agricultural Science, Tohoku University, Amamiya-machi, Aoba-ku, Sendai 981-8555, Japan,1 and Department of Biochemistry, Wake Forest University Medical School, Winston-Salem, North Carolina 271572

Received 15 February 2000/Accepted 20 April 2000

We have previously identified and characterized the alkyl hydroperoxide reductase of Streptococcus mutans, which consists of two components, Nox-1 and AhpC. Deletion of both nox-1 and ahpC had no effect on the sensitivity of S. mutans to cumene hydroperoxide or H2O2, implying that the existence of another antioxidant system(s) independent of the Nox-1-AhpC system compensates for the deficiency. Here, a new antioxidant gene (dpr for Dps-like peroxide resistance gene) was isolated from the S. mutans chromosome by its ability to complement an ahpCF deletion mutant of Escherichia coli with a tert-butyl hydroperoxide-hypersensitive phenotype. The dpr gene complemented the defect in peroxidase activity caused by the deletion of nox-1 and ahpC in S. mutans. Under aerobic conditions, the dpr disruption mutant carrying a spectinomycin resistance gene (dpr::Spcr mutant) grew as well as wild-type S. mutans in liquid medium. However, the dpr::Spcr mutant could not form colonies on an agar plate under air. In addition, neither the dpr::Spcr ahpC::Emr::nox-1 triple mutant nor the dpr::Spcr sod::Emr double mutant was able to grow aerobically in liquid medium. The 20-kDa dpr gene product Dpr is an iron-binding protein. Synthesis of Dpr was induced by exposure of S. mutans cells to air. We propose a mechanism by which Dpr confers aerotolerance on S. mutans.

* Corresponding author. Mailing address: Laboratory of Applied Microbiology, Department of Molecular and Cell Biology, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumi-dori, Amamiya-machi, Aoba-ku, Sendai 981-8555, Japan. Phone: 81-22-717-8779. Fax: 81-22-717-8780. E-mail: ykamio{at}biochem.tohoku.ac.jp.

Journal of Bacteriology, July 2000, p. 3740-3747, Vol. 182, No. 13
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Tsou, C.-C., Chiang-Ni, C., Lin, Y.-S., Chuang, W.-J., Lin, M.-T., Liu, C.-C., Wu, J.-J. (2008). An Iron-Binding Protein, Dpr, Decreases Hydrogen Peroxide Stress and Protects Streptococcus pyogenes against Multiple Stresses. Infect. Immun. 76: 4038-4045 [Abstract] [Full Text]  
  • Pulliainen, A. T., Hytonen, J., Haataja, S., Finne, J. (2008). Deficiency of the Rgg Regulator Promotes H2O2 Resistance, AhpCF-Mediated H2O2 Decomposition, and Virulence in Streptococcus pyogenes. J. Bacteriol. 190: 3225-3235 [Abstract] [Full Text]  
  • Castruita, M., Saito, M., Schottel, P. C., Elmegreen, L. A., Myneni, S., Stiefel, E. I., Morel, F. M. M. (2006). Overexpression and Characterization of an Iron Storage and DNA-Binding Dps Protein from Trichodesmium erythraeum. Appl. Environ. Microbiol. 72: 2918-2924 [Abstract] [Full Text]  
  • Pieterse, B., Leer, R. J., Schuren, F. H. J., van der Werf, M. J. (2005). Unravelling the multiple effects of lactic acid stress on Lactobacillus plantarum by transcription profiling. Microbiology 151: 3881-3894 [Abstract] [Full Text]  
  • Ceci, P., Ilari, A., Falvo, E., Giangiacomo, L., Chiancone, E. (2005). Reassessment of Protein Stability, DNA Binding, and Protection of Mycobacterium smegmatis Dps. J. Biol. Chem. 280: 34776-34785 [Abstract] [Full Text]  
  • Park, S., You, X., Imlay, J. A. (2005). Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx- mutants of Escherichia coli. Proc. Natl. Acad. Sci. USA 102: 9317-9322 [Abstract] [Full Text]  
  • Yamamoto, Y., Fukui, K., Koujin, N., Ohya, H., Kimura, K., Kamio, Y. (2004). Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutans. J. Bacteriol. 186: 5997-6002 [Abstract] [Full Text]  
  • Thibessard, A., Borges, F., Fernandez, A., Gintz, B., Decaris, B., Leblond-Bourget, N. (2004). Identification of Streptococcus thermophilus CNRZ368 Genes Involved in Defense against Superoxide Stress. Appl. Environ. Microbiol. 70: 2220-2229 [Abstract] [Full Text]  
  • Ceci, P., Ilari, A., Falvo, E., Chiancone, E. (2003). The Dps Protein of Agrobacterium tumefaciens Does Not Bind to DNA but Protects It toward Oxidative Cleavage: X-RAY CRYSTAL STRUCTURE, IRON BINDING, AND HYDROXYL-RADICAL SCAVENGING PROPERTIES. J. Biol. Chem. 278: 20319-20326 [Abstract] [Full Text]  
  • Robertson, G. T., Ng, W.-L., Gilmour, R., Winkler, M. E. (2003). Essentiality of clpX, but Not clpP, clpL, clpC, or clpE, in Streptococcus pneumoniae R6. J. Bacteriol. 185: 2961-2966 [Abstract] [Full Text]  
  • Ueshima, J., Shoji, M., Ratnayake, D. B., Abe, K., Yoshida, S., Yamamoto, K., Nakayama, K. (2003). Purification, Gene Cloning, Gene Expression, and Mutants of Dps from the Obligate Anaerobe Porphyromonas gingivalis. Infect. Immun. 71: 1170-1178 [Abstract] [Full Text]  
  • Pulliainen, A. T., Haataja, S., Kahkonen, S., Finne, J. (2003). Molecular Basis of H2O2 Resistance Mediated by Streptococcal Dpr. DEMONSTRATION OF THE FUNCTIONAL INVOLVEMENT OF THE PUTATIVE FERROXIDASE CENTER BY SITE-DIRECTED MUTAGENESIS IN STREPTOCOCCUS SUIS. J. Biol. Chem. 278: 7996-8005 [Abstract] [Full Text]  
  • Ishikawa, T., Mizunoe, Y., Kawabata, S.-i., Takade, A., Harada, M., Wai, S. N., Yoshida, S.-i. (2003). The Iron-Binding Protein Dps Confers Hydrogen Peroxide Stress Resistance to Campylobacter jejuni. J. Bacteriol. 185: 1010-1017 [Abstract] [Full Text]  
  • Ajdic', D., McShan, W. M., McLaughlin, R. E., Savic', G., Chang, J., Carson, M. B., Primeaux, C., Tian, R., Kenton, S., Jia, H., Lin, S., Qian, Y., Li, S., Zhu, H., Najar, F., Lai, H., White, J., Roe, B. A., Ferretti, J. J. (2002). Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen. Proc. Natl. Acad. Sci. USA 99: 14434-14439 [Abstract] [Full Text]  
  • Olczak, A. A., Olson, J. W., Maier, R. J. (2002). Oxidative-Stress Resistance Mutants of Helicobacter pylori. J. Bacteriol. 184: 3186-3193 [Abstract] [Full Text]  
  • Yamamoto, Y., Poole, L. B., Hantgan, R. R., Kamio, Y. (2002). An Iron-Binding Protein, Dpr, from Streptococcus mutans Prevents Iron-Dependent Hydroxyl Radical Formation In Vitro. J. Bacteriol. 184: 2931-2939 [Abstract] [Full Text]  
  • Tseng, H.-J., McEwan, A. G., Paton, J. C., Jennings, M. P. (2002). Virulence of Streptococcus pneumoniae: PsaA Mutants Are Hypersensitive to Oxidative Stress. Infect. Immun. 70: 1635-1639 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»