Disease relevance of dps

• In freshwater, rpoS and katE katG dps mutants did not show a drastic difference in sensitivity to light suggesting that osmolarity sensitizes E. coli to those deleterious effects of visible light that are unrelated to H2O2 [1].
• Agrobacterium tumefaciens Dps (DNA-binding proteins from starved cells), encoded by the dps gene located on the circular chromosome of this plant pathogen, was cloned, and its structural and functional properties were determined in vitro [2].
• Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor sigmaB in Bacillus subtilis [3].
• Reduced numbers of dps mutant bacteria in the livers and spleens of infected mice are consistent with a role of Dps in protecting Salmonella from oxidative stress encountered during infection [4].
• By genomic library tagging, we cloned a dps (stands for DNA-binding protein from starved cells) gene of the symbiotic "Candidatus Legionella jeonii" organism (called the X bacterium) (dps(X)) that grows in Amoeba proteus [5].

High impact information on dps

• One critical protein was Dps, an iron-sequestration protein, because Hpx- dps mutants exhibited sensitivity similar to that of the Hpx- oxyR mutant [6].
• The dps Gene of Symbiotic "Candidatus Legionella jeonii" in Amoeba proteus Responds to Hydrogen Peroxide and Phagocytosis [5].
• RpoS is a regulatory element for osmY and dps [7].
• Maximal induction ranged from 4.6- to 86.5-fold, for gorA and dps, respectively [8].
• This transcriptional up-regulation was preserved in a strain with the DeltaoxyR::kan mutation, but it was abolished (ahpCF) or significantly reduced (oxyR and dps) in a strain with the rpoS::Tn10 mutation, potentially reflecting positive transcriptional regulation of the oxyR regulon by sigmaS [8].

Biological context of dps

• We describe Escherichia coli survival following neutrophil phagocytosis among three mutants deleted respectively for araB, dps or oxyR [9].
• Contribution of dps to acid stress tolerance and oxidative stress tolerance in Escherichia coli O157:H7 [10].
• The sites of polyadenylation were found to be primarily in the 3'-untranslated region, either at the putative rho-independent transcription termination site (dps) or at several different sites upstream of the putative rho-independent terminator [11].
• Deletion of 164 bp of the upstream region, which included these consensus sequences, did not affect starvation-or osmotic stress-mediated induction of pexB but abolished its induction by oxidative stress [12].
• The pexB upstream region contained 245 nucleotides within which sequences approximating the consensus for cyclic AMP receptor protein and integration host factor binding sites were discernible [12].

Associations of dps with chemical compounds

• The appearance of Arg(+) mutants on the plates with streptomycin was not significantly altered by recA, rpoS or dps mutations [13].
• Both the dps1 (formerly dps) and dlp1 mutants could generate ubiquinone when they were transformed with a bacterial decaprenyl diphosphate synthase, which functions in its host as a homodimer [14].

Other interactions of dps

• Single-copy pexB-lacZ operon fusions were constructed to study transcriptional regulation and the promoter region of this gene [12].
• We also assayed the effect on gyrB expression in strains containing mutations in either smc or dps, two genes encoding proteins that condense DNA [15].

Analytical, diagnostic and therapeutic context of dps

• Fluorescence in situ hybridization using fluorochrome-labeled oligonucleotide probes was used to measure the cellular concentration of fis and dps mRNA [16].

References