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An Iron-Binding Protein, Dpr, from Streptococcus mutans Prevents Iron-Dependent Hydroxyl Radical Formation In Vitro. Yuji Yamamoto, 2002.The dpr gene is an antioxidant gene which was isolated from the Streptococcus mutans chromosome by its ability to complement an alkyl hydroperoxide reductase-deficient mutant of Escherichia coli, and it was proven to play an indispensable role in oxygen tolerance in S . mutans . Here, we purified the 20-kDa dpr gene product, Dpr, from a crude extract of S . mutans as an iron-binding protein and found that Dpr formed a spherical oligomer about 9 nm in diameter . Molecular weight determinations of Dpr in solution by analytical ultracentrifugation and light-scattering analyses gave values of 223,000 to 292,000, consistent with a subunit composition of 11.5 to 15 subunits per molecule . The purified Dpr contained iron and zinc atoms and had an ability to incorporate up to 480 iron and 11.2 zinc atoms per molecule . Unlike E . coli Dps and two other members of the Dps family, Dpr was unable to bind DNA . One hundred nanomolar Dpr prevented by more than 90% the formation of hydroxyl radical generated by 10 µM iron(II) salt in vitro . The data shown in this study indicate that Dpr may act as a ferritin-like iron-binding protein in S . mutans and may allow this catalase- and heme-peroxidase-deficient bacterium to grow under air by limiting the iron-catalyzed Fenton reaction . Genes Encoding Specific Nickel Transport Systems Flank the Chromosomal Urease Locus of Pathogenic Yersiniae. Florent Sebbane, 2002.The transition metal nickel is an essential cofactor for a number of bacterial enzymes, one of which is urease . Prior to its incorporation into metalloenzyme active sites, nickel must be imported into the cell . Here, we report identification of two loci corresponding to nickel-specific transport systems in the gram-negative, ureolytic bacterium Yersinia pseudotuberculosis . The loci are located on each side of the chromosomal urease gene cluster ureABCEFGD and have the same orientation as the latter . The yntABCDE locus upstream of the ure genes encodes five predicted products with sequence homology to ATP-binding cassette nickel permeases present in several gram-negative bacteria . The ureH gene, located downstream of ure, encodes a single-component carrier which displays homology to polypeptides of the nickel-cobalt transporter family . Transporters with homology to these two classes are also present (again in proximity to the urease locus) in the other two pathogenic yersiniae, Y . pestis and Y . enterocolitica . An Escherichia coli nikA insertion mutant recovered nickel uptake ability following heterologous complementation with either the ynt or the ureH plasmid-borne gene of Y . pseudotuberculosis, demonstrating that each carrier is necessary and sufficient for nickel transport . Deletion of ynt in Y . pseudotuberculosis almost completely abolished bacterial urease activity, whereas deletion of ureH had no effect . Nevertheless, rates of nickel transport were significantly altered in both ynt and ureH mutants . Furthermore, the ynt ureH double mutant was totally devoid of nickel uptake ability, thus indicating that Ynt and UreH constitute the only routes for nickel entry . Both Ynt and UreH show selectivity for Ni2+ ions . This is the first reported identification of genes coding for both kinds of nickel-specific permeases situated adjacent to the urease gene cluster in the genome of a microorganism .
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