Crystal Structure of Streptococcus suis Dps-like Peroxide Resistance Protein Dpr: Implications for Iron Incorporation

Kauko, Anni; Haataja, Sauli; Pulliainen, Arto T.; Finne, Jukka; Papageorgiou, Anastassios C.

doi:10.1016/j.jmb.2004.03.009

Cited by 48 publications

(70 citation statements)

References 58 publications

(41 reference statements)

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“…It was also reported that some Dps family proteins having iron binding, but not DNAbinding ability, were involved in oxidative stress resistance (8,16,28). The crystal structure of Dps family proteins, including Streptococcus suis Dpr homologue, revealed a ferritin-like structure of the proteins, indicating that this class of proteins could incorporate iron ions as ferritin does (8,10,14,18,38). Taken together with our data on Dpr properties, it was suggested that Dps family proteins could affect the cellular free iron ion status, thereby conferring oxygen tolerance.…”

supporting

confidence: 61%

Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutans

Yamamoto¹,

Fukui

Koujin³

et al. 2004

J Bacteriol

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). 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 M, 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 M; under these conditions, dpr mutant cells maintained intracellular iron concentration at 230.3 ؎ 28.8 M. 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.

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supporting

confidence: 61%

Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutans

Yamamoto¹,

Fukui

Koujin³

et al. 2004

J Bacteriol

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“…In all previously characterized Dps proteins, this redox reaction is mediated by a unique diiron-binding motif (Fig. 11) (16,33,36,37,41). This motif has been implicated in coordinating the two-electron reduction of H 2 O 2.…”

Section: Discussionmentioning

confidence: 99%

An archaeal antioxidant: Characterization of a Dps-like protein from Sulfolobus solfataricus

Wiedenheft

Mosolf

Willits

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

107

110

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Evolution of an oxygenic atmosphere required primordial life to accommodate the toxicity associated with reactive oxygen species. We have characterized an archaeal antioxidant from the hyperthermophilic acidophile Sulfolobus solfataricus. The amino acid sequence of this Ϸ22-kDa protein shares little sequence similarity with proteins with known function. However, the protein shares high sequence similarity with hypothetical proteins in other archaeal and bacterial genomes. Nine of these hypothetical proteins form a monophyletic cluster within the broad superfamily of ferritin-like diiron-carboxylate proteins. Higher order structural predictions and image reconstructions indicate that the S. solfataricus protein is structurally related to a class of DNA-binding protein from starved cells (Dps). The recombinant protein self assembles into a hollow dodecameric protein cage having tetrahedral symmetry (SsDps). The outer shell diameter is Ϸ10 nm, and the interior diameter is Ϸ5 nm. Dps proteins have been shown to protect nucleic acids by physically shielding DNA against oxidative damage and by consuming constituents involved in Fenton chemistry. In vitro, the assembled archaeal protein efficiently uses H2O2 to oxidize Fe(II) to Fe(III) and stores the oxide as a mineral core on the interior surface of the protein cage. The ssdps gene is upregulated in S. solfataricus cultures grown in iron-depleted media and upon H2O2 stress, but is not induced by other stresses. SsDps-mediated reduction of hydrogen peroxide and possible DNA-binding capabilities of this archaeal Dps protein are mechanisms by which S. solfataricus mitigates oxidative damage.ferritin ͉ iron ͉ oxidative stress ͉ biomineralization ͉ hyperthermophile

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“…A homolog of Dps, Dpr (Dps-like peroxide resistance), is conserved in Gram-positive bacteria, such as Streptococcus mutans, Streptococcus pyogenes, and Streptococcus suis (11)(12)(13). The structure of Dpr from S. suis is similar to that of Dps, and it can bind ferrous ions as well as other divalent cations, such as Cu 2ϩ , Mn 2ϩ , and Zn 2ϩ (14,15). Dpr is essential for aerobic survival of S. mutans and also prevents iron-dependent hydroxyl radical formation in vitro (16).…”

mentioning

confidence: 99%

Effect of Nonheme Iron-Containing Ferritin Dpr in the Stress Response and Virulence of Pneumococci

et al. 2014

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bStreptococcus pneumoniae (pneumococcus) produces hydrogen peroxide as a by-product of metabolism and provides a competitive advantage against cocolonizing bacteria. As pneumococci do not produce catalase or an inducible regulator of hydrogen peroxide, the mechanism of resistance to hydrogen peroxide is unclear. A gene responsible for resistance to hydrogen peroxide and iron in other streptococci is that encoding nonheme iron-containing ferritin, dpr, but previous attempts to study this gene in pneumococcus by generating a dpr mutant were unsuccessful. In the current study, we found that dpr is in an operon with the downstream genes dhfr and clpX. We generated a dpr deletion mutant which displayed normal early-log-phase and mid-logphase growth in bacteriologic medium but survived less well at stationary phase; the addition of catalase partially rescued the growth defect. We showed that the dpr mutant is significantly more sensitive to pH, heat, iron concentration, and oxidative stress due to hydrogen peroxide. Using a mouse model of colonization, we also showed that the dpr mutant displays a reduced ability to colonize and is more rapidly cleared from the nasopharynx. Our results thus suggest that Dpr is important for pneumococcal resistance to stress and for nasopharyngeal colonization.

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Crystal Structure of Streptococcus suis Dps-like Peroxide Resistance Protein Dpr: Implications for Iron Incorporation

Cited by 48 publications

References 58 publications

Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutans

Regulation of the Intracellular Free Iron Pool by Dpr Provides Oxygen Tolerance to Streptococcus mutans

An archaeal antioxidant: Characterization of a Dps-like protein from Sulfolobus solfataricus

Effect of Nonheme Iron-Containing Ferritin Dpr in the Stress Response and Virulence of Pneumococci

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