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Gene Review

fur  -  ferric uptake regulator

Escherichia coli O157:H7 str. Sakai

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Disease relevance of fur


High impact information on fur


Chemical compound and disease context of fur


Biological context of fur


Associations of fur with chemical compounds

  • NO was recently shown to react with Fe(2+) ions in FeFur (iron substituted Fur protein) leading to an Fur bound iron-nitrosyl complex, unable to bind DNA, and characterized by a g = 2.03 EPR signal, associated with an S = (1)/(2) ground state [2].
  • The use of several spectroscopic tools such as EPR, ENDOR, FTIR, Mössbauer, and UV-visible spectroscopies as well as mass spectrometry analysis was necessary to characterize the iron-nitrosyl species in Fur [2].
  • The iron-bound form of Fur has proved difficult to obtain, and conflicting results have been published using Mn(II) as a probe for in vitro DNA-binding studies [9].
  • Ethylation interference experiments demonstrate that there are relatively few phosphate contacts of unique disposition while hydroxyl radical footprinting demonstrates that Fur-operator contacts are segregated on one face of the helix and span nearly three successive major grooves [15].
  • The mutant (UV14) was found to harbour two altered loci: one is in the trans-regulatory gene fnr (fumarate nitrate reduction) where leucine-129 was changed to glutamine (fnr14), and the second (sodA14) is in the promoter region (cis) of the sodA gene apparently affecting the binding of the Fur (ferric uptake regulation) protein [16].

Regulatory relationships of fur


Analytical, diagnostic and therapeutic context of fur


  1. Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron. D'Autreaux, B., Touati, D., Bersch, B., Latour, J.M., Michaud-Soret, I. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  2. Spectroscopic description of the two nitrosyl-iron complexes responsible for fur inhibition by nitric oxide. D'Autréaux, B., Horner, O., Oddou, J.L., Jeandey, C., Gambarelli, S., Berthomieu, C., Latour, J.M., Michaud-Soret, I. J. Am. Chem. Soc. (2004) [Pubmed]
  3. Role of the ferric uptake regulator of Pseudomonas aeruginosa in the regulation of siderophores and exotoxin A expression: purification and activity on iron-regulated promoters. Ochsner, U.A., Vasil, A.I., Vasil, M.L. J. Bacteriol. (1995) [Pubmed]
  4. Iron regulation and pathogenicity in Erwinia chrysanthemi 3937: role of the Fur repressor protein. Franza, T., Sauvage, C., Expert, D. Mol. Plant Microbe Interact. (1999) [Pubmed]
  5. Cloning, overexpression and interaction of recombinant Fur from the cyanobacterium Anabaena PCC 7119 with isiB and its own promoter. Bes, M.T., Hernández, J.A., Peleato, M.L., Fillat, M.F. FEMS Microbiol. Lett. (2001) [Pubmed]
  6. Purification and characterization of the diphtheria toxin repressor. Schmitt, M.P., Twiddy, E.M., Holmes, R.K. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  7. Evidence of an unusually long operator for the fur repressor in the aerobactin promoter of Escherichia coli. Escolar, L., Pérez-Martín, J., de Lorenzo, V. J. Biol. Chem. (2000) [Pubmed]
  8. Spectroscopic and saturation magnetization properties of the manganese- and cobalt-substituted Fur (ferric uptake regulation) protein from Escherichia coli. Adrait, A., Jacquamet, L., Le Pape, L., Gonzalez de Peredo, A., Aberdam, D., Hazemann, J.L., Latour, J.M., Michaud-Soret, I. Biochemistry (1999) [Pubmed]
  9. The ferric uptake regulation (Fur) repressor is a zinc metalloprotein. Althaus, E.W., Outten, C.E., Olson, K.E., Cao, H., O'Halloran, T.V. Biochemistry (1999) [Pubmed]
  10. Expression, isolation and properties of Fur (ferric uptake regulation) protein of Escherichia coli K 12. Wee, S., Neilands, J.B., Bittner, M.L., Hemming, B.C., Haymore, B.L., Seetharam, R. Biology of metals. (1988) [Pubmed]
  11. Structural changes of Escherichia coli ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography. Pecqueur, L., D'Autréaux, B., Dupuy, J., Nicolet, Y., Jacquamet, L., Brutscher, B., Michaud-Soret, I., Bersch, B. J. Biol. Chem. (2006) [Pubmed]
  12. Metalloregulation in vitro of the aerobactin promoter of Escherichia coli by the Fur (ferric uptake regulation) protein. Escolar, L., de Lorenzo, V., Pérez-Martín, J. Mol. Microbiol. (1997) [Pubmed]
  13. Mechanism and regulation of synthesis of aerobactin in Escherichia coli K12 (pColV-K30). Neilands, J.B. Can. J. Microbiol. (1992) [Pubmed]
  14. The Rhizobium leguminosarum regulator IrrA affects the transcription of a wide range of genes in response to Fe availability. Todd, J.D., Sawers, G., Rodionov, D.A., Johnston, A.W. Mol. Genet. Genomics (2006) [Pubmed]
  15. The interaction of the ferric uptake regulation protein with DNA. Coy, M. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  16. Characterization of regulatory mutations causing anaerobic derepression of the sodA gene in Escherichia coli K12: cooperation between cis- and trans-acting regulatory loci. Beaumont, M.D., Hassan, H.M. J. Gen. Microbiol. (1993) [Pubmed]
  17. Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus. Niederhoffer, E.C., Naranjo, C.M., Bradley, K.L., Fee, J.A. J. Bacteriol. (1990) [Pubmed]
  18. Mechanism for iron-regulated transcription of the Escherichia coli cir gene: metal-dependent binding of fur protein to the promoters. Griggs, D.W., Konisky, J. J. Bacteriol. (1989) [Pubmed]
  19. Fur (ferric uptake regulation) protein interaction with target DNA: comparison of gel retardation, footprinting and electron microscopy analyses. Fréchon, D., Le Cam, E. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  20. Site-directed mutagenesis of the ferric uptake regulation gene of Escherichia coli. Coy, M., Doyle, C., Besser, J., Neilands, J.B. Biometals (1994) [Pubmed]
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