Kôichi Fukui,2 Naoko Koujin,1 Hiroaki Ohya,2 Kazuhiko Kimura,3 and Yoshiyuki Kamio1*
Department of Microbial Biotechnology,1 Division of Biological Resource Science, Graduate School of Agricultural Science, Tohoku University, Aoba-ku, Sendai,3 Yamagata Public Corporation for the Development of Industry, Yamagata, Japan2
Received 23 February 2004/ Accepted 22 March 2004
Dpr is an iron-binding protein required for oxygen tolerance in Streptococcus mutans. We previously proposed that Dpr could confer oxygen tolerance to the bacterium by sequestering intracellular free iron ions that catalyze generation of highly toxic radicals (Y. Yamamoto, M. Higuchi, L. B. Poole, and Y. Kamio, J. Bacteriol. 182:3740-3747, 2000; Y. Yamamoto, L. B. Poole, R. R. Hantgan, and Y. Kamio, J. Bacteriol. 184:2931-2939, 2002). Here, we examined the intracellular free iron status of wild-type (WT) and dpr mutant strains of S. mutans, before and after exposure to air, by using electron spin resonance spectrometry. Under anaerobic conditions, free iron ion concentrations of WT and dpr strains were 225.9 ± 2.6 and 333.0 ± 61.3 µM, respectively. Exposure of WT cells to air for 1 h induced Dpr expression and reduced intracellular free iron ion concentrations to 22.5 ± 5.3 µM; under these conditions, dpr mutant cells maintained intracellular iron concentration at 230.3 ± 28.8 µM. A decrease in cell viability and genomic DNA degradation was observed in the dpr mutant exposed to air. These data indicate that regulation of the intracellular free iron pool by Dpr is required for oxygen tolerance in S. mutans.
Present address: Unité de Recherches Laitières et Génétique AppliquéeURLGA, Institut National de la Recherche Agronomique, Domaine de Vilvert, Jouy en Josas, France.
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