The multifaceted capacity of Dps proteins to combat bacterial stress conditions: Detoxification of iron and hydrogen peroxide and DNA binding

Chiancone, Emilia; Ceci, Pierpaolo

doi:10.1016/j.bbagen.2010.01.013

Cited by 186 publications

(198 citation statements)

References 57 publications

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“…Wildtype DPS protein formed solely 12-mer, consistent with the literature. 18,25,26 All the DPS single mutants assembled into 12-mers but four mutants also formed smaller oligomers. Mutation of W52 resulted in some unassembled monomer (6%) and the mutant Y16A formed a small amount (16%) of dimer along with 12-mer.…”

Section: Size Exclusion Chromatographic Determination Of Assembly In mentioning

confidence: 99%

Rational disruption of the oligomerization of the mini‐ferritin E. coli DPS through protein‐protein interface mutation

Zhang

Chee

et al. 2011

Protein Science

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DNA-binding protein from starved cells (DPS), a mini-ferritin capable of self-assembling into a 12-meric nano-cage, was chosen as the basis for an alanine-shaving mutagenesis study to investigate the importance of key amino acid residues, located at symmetry-related protein-protein interfaces, in controlling protein stability and self-assembly. Nine mutants were designed through simple inspection, synthesized, and subjected to transmission electron microscopy, circular dichroism, size exclusion chromatography, and ''virtual alanine scanning'' computational analysis. The data indicate that many of these residues may be hot spot residues. Most remarkably, two residues, R83 and R133, were observed to shift the oligomerization state to~50% dimer. Based on the hypothesis that these two residues constitute a ''hot strip,'' located at the ferritin-like threefold axis, the double mutant was generated which completely shuts down detectable formation of 12-mer in solution, favoring a cooperatively folded dimer. The fact that this effect logically builds upon the single mutants emphasizes that complex self-assembly has the potential to be manipulated rationally. This study should have an impact on the fundamental understanding of the assembly of DPS protein cages specifically and protein quaternary structure in general. In addition, as there is much interest in applying these and similar systems to the templation of nano-materials and drug delivery, the ability to control this ferritin's oligomerization state and stability could prove especially valuable.

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Section: Size Exclusion Chromatographic Determination Of Assembly In mentioning

confidence: 99%

Rational disruption of the oligomerization of the mini‐ferritin E. coli DPS through protein‐protein interface mutation

Zhang

Chee

et al. 2011

Protein Science

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“…1b, c). The Dps FOC is known to contain two metal-binding sites with a different affinity for Fe 2+ ions (Franceschini et al, 2006 (Chiancone & Ceci, 2010). In Escherichia coli Dps, the reaction rate increases 100-fold in the presence of H 2 O 2 (Zhao et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

“…Dps proteins are widely distributed in prokaryotes (Chiancone & Ceci, 2010), being required for survival during stressful conditions such as nutrient starvation, thermal stress and oxidative conditions, and inside biofilm (Almiró n et al, 1992;Dundon et al, 2001;Martinez & Kolter, 1997;Nair & Finkel, 2004;Pang et al, 2012;Theoret et al, 2011). The archetypical function of Dps seems to be DNA protection against hydroxyl radicals that are produced when Fe 2+ and H 2 O 2 combine (Zhao et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Conserved histidine residues at the ferroxidase centre of the Campylobacter jejuni Dps protein are not strictly required for metal binding and oxidation

Sanchuki¹,

Valdameri²,

Moure³

et al. 2016

Microbiology

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Iron is an essential micronutrient for living organisms as it is involved in a broad variety of important biological processes. However, free iron inside the cell could be potentially toxic, generating hydroxyl radicals through the Fenton reaction. Dps (DNA-binding protein from starved cells) belongs to a subfamily of ferritins and can store iron atoms inside the dodecamer. The presence of a ferroxidase centre, composed of highly conserved residues, is a signature of this protein family. In this study, we analysed the role of two conserved histidine residues (H25 and H37) located at the ferroxidase centre of the Campylobacter jejuni Dps protein by replacing them with glycine residues. The C. jejuni H25G/H37G substituted variant showed reduced iron binding and ferroxidase activities in comparison with wt Dps, while DNA-binding activity remained unaffected. We also found that both CjDps wt and CjDps H25G/H37G were able to bind manganese atoms. These results indicate that the H25 and H37 residues at the ferroxidase centre of C. jejuni Dps are not strictly required for metal binding and oxidation.

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“…These enhancements would increase cell growth and reduce the cost of commercialized probiotic products. Most LAB strains lack catalase, cytochrome and heme-containing proteins (Chiancone and Ceci, 2010), which protect against oxidative stress or oxygen toxicity. Physiological adaptation to oxidative stress in aerobic microorganisms requires enzymatic defense against oxidative stress, examples of which include catalase, superoxide dismutase (SOD), glutathione reductase and peroxidase (Jänsch et al, 2011).…”

mentioning

confidence: 99%

Enhancement of biomass production and nutrition utilization by strain Lactobacillus acidophilus DGK derived from serial subculturing in an aerobic environment

Hwang¹,

Lin²,

Yan³

et al. 2015

Afr. J. Biotechnol.

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The multifaceted capacity of Dps proteins to combat bacterial stress conditions: Detoxification of iron and hydrogen peroxide and DNA binding

Cited by 186 publications

References 57 publications

Rational disruption of the oligomerization of the mini‐ferritin E. coli DPS through protein‐protein interface mutation

Rational disruption of the oligomerization of the mini‐ferritin E. coli DPS through protein‐protein interface mutation

Conserved histidine residues at the ferroxidase centre of the Campylobacter jejuni Dps protein are not strictly required for metal binding and oxidation

Enhancement of biomass production and nutrition utilization by strain Lactobacillus acidophilus DGK derived from serial subculturing in an aerobic environment

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