HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 10, 7996-8005, March 7, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/10/7996    most recent M210174200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pulliainen, A. T. Articles by Finne, J. Search for Related Content PubMed PubMed Citation Articles by Pulliainen, A. T. Articles by Finne, J. Social Bookmarking                      What's this?

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^*

Arto Tapio Pulliainen, Sauli Haataja, Sanni Kähkönen, and Jukka Finne

From the Department of Medical Biochemistry and Molecular Biology, University of Turku, FIN-20520 Turku, Finland

H₂O₂ is an unavoidable cytotoxic by-product of aerobic life. Dpr, a recently discovered member of the Dps protein family, provides a means for catalase-negative bacteria to tolerate H₂O₂. Potentially, Dpr could bind free intracellular iron and thus inhibit the Fenton chemistry-catalyzed formation of toxic hydroxyl radicals (H₂O₂ + Fe^{2+  ·}OH + ^-OH + Fe³⁺). We explored the in vivo function of Dpr in the catalase- and NADH peroxidase-negative pig and human pathogen Streptococcus suis. We show that: (i) a Dpr allelic exchange knockout mutant was hypersensitive (~10⁶-fold) to H₂O₂, (ii) Dpr incorporated iron in vivo, (iii) a putative ferroxidase center was present in Dpr, (iv) single amino acid substitutions D74A or E78A to the putative ferroxidase center abolished the in vivo iron incorporation, and (v) the H₂O₂ hypersensitive phenotype was complemented by wild-type Dpr or by a membrane-permeating iron chelator, but not by the site-mutated forms of Dpr. These results demonstrate that the putative ferroxidase center of Dpr is functionally active in iron incorporation and that the H₂O₂ resistance is mediated by Dpr in vivo by its iron binding activity.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY154459.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				V. Loimaranta, J. Hytonen, A. T. Pulliainen, A. Sharma, J. Tenovuo, N. Stromberg, and J. Finne Leucine-rich Repeats of Bacterial Surface Proteins Serve as Common Pattern Recognition Motifs of Human Scavenger Receptor gp340 J. Biol. Chem., July 10, 2009; 284(28): 18614 - 18623. [Abstract] [Full Text] [PDF]

				L. Herve-Jimenez, I. Guillouard, E. Guedon, S. Boudebbouze, P. Hols, V. Monnet, E. Maguin, and F. Rul Postgenomic Analysis of Streptococcus thermophilus Cocultivated in Milk with Lactobacillus delbrueckii subsp. bulgaricus: Involvement of Nitrogen, Purine, and Iron Metabolism Appl. Envir. Microbiol., April 1, 2009; 75(7): 2062 - 2073. [Abstract] [Full Text] [PDF]

				Y. Feng, M. Li, H. Zhang, B. Zheng, H. Han, C. Wang, J. Yan, J. Tang, and G. F. Gao Functional Definition and Global Regulation of Zur, a Zinc Uptake Regulator in a Streptococcus suis Serotype 2 Strain Causing Streptococcal Toxic Shock Syndrome J. Bacteriol., November 15, 2008; 190(22): 7567 - 7578. [Abstract] [Full Text] [PDF]

				C.-C. Tsou, C. Chiang-Ni, Y.-S. Lin, W.-J. Chuang, M.-T. Lin, C.-C. Liu, and J.-J. Wu An Iron-Binding Protein, Dpr, Decreases Hydrogen Peroxide Stress and Protects Streptococcus pyogenes against Multiple Stresses Infect. Immun., September 1, 2008; 76(9): 4038 - 4045. [Abstract] [Full Text] [PDF]

				A. T. Pulliainen, J. Hytonen, S. Haataja, and J. Finne Deficiency of the Rgg Regulator Promotes H2O2 Resistance, AhpCF-Mediated H2O2 Decomposition, and Virulence in Streptococcus pyogenes J. Bacteriol., May 1, 2008; 190(9): 3225 - 3235. [Abstract] [Full Text] [PDF]

				W.-L. Ng, H.-C. T. Tsui, and M. E. Winkler Regulation of the pspA Virulence Factor and Essential pcsB Murein Biosynthetic Genes by the Phosphorylated VicR (YycF) Response Regulator in Streptococcus pneumoniae J. Bacteriol., November 1, 2005; 187(21): 7444 - 7459. [Abstract] [Full Text] [PDF]

				P. Ceci, A. Ilari, E. Falvo, L. Giangiacomo, and E. Chiancone Reassessment of Protein Stability, DNA Binding, and Protection of Mycobacterium smegmatis Dps J. Biol. Chem., October 14, 2005; 280(41): 34776 - 34785. [Abstract] [Full Text] [PDF]

				M. I. Pajunen, A. T. Pulliainen, J. Finne, and H. Savilahti Generation of transposon insertion mutant libraries for Gram-positive bacteria by electroporation of phage Mu DNA transposition complexes Microbiology, April 1, 2005; 151(4): 1209 - 1218. [Abstract] [Full Text] [PDF]

				K. N. Olsen, M. H. Larsen, C. G. M. Gahan, B. Kallipolitis, X. A. Wolf, R. Rea, C. Hill, and H. Ingmer The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells Microbiology, March 1, 2005; 151(3): 925 - 933. [Abstract] [Full Text] [PDF]

				A. T. Ulijasz, D. R. Andes, J. D. Glasner, and B. Weisblum Regulation of Iron Transport in Streptococcus pneumoniae by RitR, an Orphan Response Regulator J. Bacteriol., December 1, 2004; 186(23): 8123 - 8136. [Abstract] [Full Text] [PDF]

				P. Ceci, S. Cellai, E. Falvo, C. Rivetti, G. L. Rossi, and E. Chiancone DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus Nucleic Acids Res., November 8, 2004; 32(19): 5935 - 5944. [Abstract] [Full Text] [PDF]

				Y. Yamamoto, K. Fukui, N. Koujin, H. Ohya, K. Kimura, and Y. Kamio Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutans J. Bacteriol., September 15, 2004; 186(18): 5997 - 6002. [Abstract] [Full Text] [PDF]