wrbA

Summary

Gene Symbol: wrbA
Description: NAD(P)H:quinone oxidoreductase
Alias: ECK0995, JW0989
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Serra Moreno R, Jofre J, Muniesa M. Insertion site occupancy by stx2 bacteriophages depends on the locus availability of the host strain chromosome. J Bacteriol. 2007;189:6645-54 pubmed
    ..For the most part, yehV is occupied in STEC strains while wrbA is preferentially selected by the same stx phages in E. coli laboratory strains...
  2. Degtjarik O, Brynda J, Ettrichová O, Kuty M, Sinha D, Kuta Smatanova I, et al. Quantum Calculations Indicate Effective Electron Transfer between FMN and Benzoquinone in a New Crystal Structure of Escherichia coli WrbA. J Phys Chem B. 2016;120:4867-77 pubmed publisher
    ..to compare the electron-transfer probability for two distinct crystal structures of the Escherichia coli protein WrbA, an FMN-dependent quinone oxidoreductase, with the bound substrate benzoquinone...
  3. Grandori R, Khalifah P, Boice J, Fairman R, Giovanielli K, Carey J. Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins. J Biol Chem. 1998;273:20960-6 pubmed
    The protein WrbA had been identified as an Escherichia coli stationary-phase protein that copurified and coimmunoprecipitated with the tryptophan repressor...
  4. Carey J, Brynda J, Wolfova J, Grandori R, Gustavsson T, Ettrich R, et al. WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases. Protein Sci. 2007;16:2301-5 pubmed
    The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1...
  5. Yang W, Ni L, Somerville R. A stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNA. Proc Natl Acad Sci U S A. 1993;90:5796-800 pubmed
    ..The second protein, designated WrbA [for tryptophan (W) repressor-binding protein] remained associated with its namesake through several sequential ..
  6. Bore E, Hebraud M, Chafsey I, Chambon C, Skjaeret C, Moen B, et al. Adapted tolerance to benzalkonium chloride in Escherichia coli K-12 studied by transcriptome and proteome analyses. Microbiology. 2007;153:935-46 pubmed
    ..The results revealed that BC treatment might result in superoxide stress in E. coli. ..
  7. Natalello A, Doglia S, Carey J, Grandori R. Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA. Biochemistry. 2007;46:543-53 pubmed
    b>WrbA is an oligomeric flavodoxin-like protein that binds one molecule of flavin mononucleotide (FMN) per monomer and whose redox activity is implicated in oxidative stress defense...
  8. Lacour S, Landini P. SigmaS-dependent gene expression at the onset of stationary phase in Escherichia coli: function of sigmaS-dependent genes and identification of their promoter sequences. J Bacteriol. 2004;186:7186-95 pubmed
    ..Only seven genes (dps, osmE, osmY, sodC, rpsV, wrbA, and yahO) had previously been recognized as rpoS dependent...
  9. Weichart D, Querfurth N, Dreger M, Hengge Aronis R. Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli. J Bacteriol. 2003;185:115-25 pubmed
    ..For example, in the clpP and clpA mutant cultures, the Dps protein, the WrbA protein, and the periplasmic lysine-arginine-ornithine binding protein ArgT did not display the induction typical ..

More Information

Publications20

  1. Kirkpatrick C, Maurer L, Oyelakin N, Yoncheva Y, Maurer R, Slonczewski J. Acetate and formate stress: opposite responses in the proteome of Escherichia coli. J Bacteriol. 2001;183:6466-77 pubmed
  2. Grandori R, Carey J. Six new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin. Protein Sci. 1994;3:2185-93 pubmed
    Strong sequence similarity has been reported among WrbA (the Trp repressor-binding protein of Escherichia coli); Ycp4, a protein of unknown function from the budding yeast Saccharomyces cerevisiae; P25, the pap1-dependent protein of the ..
  3. Gorman J, Shapiro L. Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide. Protein Sci. 2005;14:3004-12 pubmed publisher
    The tryptophan repressor binding protein WrbA binds to the tryptophan repressor protein TrpR. Although the biological role of WrbA remains unclear, it has been proposed to function in enhancing the stability of TrpR-DNA complexes...
  4. Nöll G, Kozma E, Grandori R, Carey J, Schödl T, Hauska G, et al. Spectroelectrochemical investigation of a flavoprotein with a flavin-modified gold electrode. Langmuir. 2006;22:2378-83 pubmed
    ..was successfully applied to the electrochemical and spectroelectrochemical investigation of the flavoprotein WrbA from Escherichia coli that shows some structural similarities to flavodoxins...
  5. Patridge E, Ferry J. WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase. J Bacteriol. 2006;188:3498-506 pubmed publisher
    b>WrbA (tryptophan [W] repressor-binding protein) was discovered in Escherichia coli, where it was proposed to play a role in regulation of the tryptophan operon; however, this has been put in question, leaving the function unknown...
  6. Liu X, De Wulf P. Probing the ArcA-P modulon of Escherichia coli by whole genome transcriptional analysis and sequence recognition profiling. J Biol Chem. 2004;279:12588-97 pubmed
    ..A conservative but reasonable assessment is that the Arc pathway recruits 100-150 operons to mediate a role in cellular adaptation that is more extensive than hitherto anticipated. ..
  7. Wolfova J, Mesters J, Brynda J, Grandori R, Natalello A, Carey J, et al. Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007;63:571-5 pubmed
    The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress...
  8. Andrade S, Patridge E, Ferry J, Einsle O. Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli. J Bacteriol. 2007;189:9101-7 pubmed
    The flavoprotein WrbA, originally described as a tryptophan (W) repressor-binding protein in Escherichia coli, has recently been shown to exhibit the enzymatic activity of a NADH:quinone oxidoreductase...
  9. Tjaden B, Goodwin S, Opdyke J, Guillier M, Fu D, Gottesman S, et al. Target prediction for small, noncoding RNAs in bacteria. Nucleic Acids Res. 2006;34:2791-802 pubmed
    ..Our results show that TargetRNA is a useful tool for finding mRNA targets of sRNAs, although its rate of success varies between sRNAs. ..
  10. Loewen P, Hu B, Strutinsky J, Sparling R. Regulation in the rpoS regulon of Escherichia coli. Can J Microbiol. 1998;44:707-17 pubmed
    ..The activity of sigma s may also be modulated by trehalose and glutamate, which activate holoenzyme formation and promote holoenzyme binding to certain promoters. ..
  11. Wolfova J, Smatanova I, Brynda J, Mesters J, Lapkouski M, Kuty M, et al. Structural organization of WrbA in apo- and holoprotein crystals. Biochim Biophys Acta. 2009;1794:1288-98 pubmed publisher
    Two previously reported holoprotein crystal forms of the flavodoxin-like E. coli protein WrbA, diffracting to 2.6 and 2.0 A resolution, and new crystals of WrbA apoprotein diffracting to 1...