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Gene Review

fhuA  -  ferrichrome outer membrane transporter

Escherichia coli CFT073

 
 
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Disease relevance of fhuA

  • Three separate sweeps, observed as classic periodic selection events causing a change in the frequency of neutral mutations (in fhuA causing phage T5 resistance), were identified with changes at particular loci [1].
  • The Escherichia coli fhu operon, composed of the fhuA, C, D, and B genes, is essential for the utilization of ferric siderophores of the hydroxamate type and for the uptake of the antibiotic albomycin [2].
  • The plasmid construct (pGR1), designed to express fhuA under the lac promoter of E. coli, complemented E. coli MB97 DeltafhuA mutant for ferri-ferrichrome utilization and also allowed Rhizobium spp [3].
 

High impact information on fhuA

  • Additional experiments showed that the insertion disrupted the fhuA gene, which encodes the multifunctional outer membrane receptor for ferrichrome, the antibiotic albomycin, colicin M, and bacteriophages T5, T1, and phi 80 [4].
  • Physical mapping of the fusion-containing plasmids confirmed the presence of three restriction sites which were also located on the chromosomal DNA of sequences near the fhuA gene [5].
  • The direction of transcription of the fhuA gene was deduced from the direction of transcription of the (fhuA'-'lacZ) gene fusion [5].
  • The genetic products were determined in maxicells and minicells. fhuA codes for the known 78,000-dalton receptor protein and the 81,000-dalton precursor in the outer membrane, fhuC codes for a 30,000-dalton protein, and fhuD encodes a 26,000-dalton protein in the cytoplasmic membrane [6].
  • The fhu genes of Rhizobium leguminosarum, specifying siderophore uptake proteins: fhuDCB are adjacent to a pseudogene version of fhuA [7].
 

Biological context of fhuA

 

Associations of fhuA with chemical compounds

  • The rhizobial transformants expressing fhuA showed growth stimulation when co-inoculated with Ustilago maydis, a fungal species known to produce ferrichrome under iron starved conditions [3].
  • Mutations in the fhuA gene usually decreased expression of the subsequent fhuC,D,B genes to such an extent that growth on ferric aerobactin as sole iron source was abolished [11].
  • Antibodies were raised against fhuA protein by injecting rabbits with isolated material in polyacrylamide chips [12].

References

  1. Experimental analysis of molecular events during mutational periodic selections in bacterial evolution. Notley-McRobb, L., Ferenci, T. Genetics (2000) [Pubmed]
  2. Transport activity of FhuA, FhuC, FhuD, and FhuB derivatives in a system free of polar effects, and stoichiometry of components involved in ferrichrome uptake. Mademidis, A., Köster, W. Mol. Gen. Genet. (1998) [Pubmed]
  3. Functional expression of Escherichia coli fhuA gene in Rhizobium spp. of Cajanus cajan provides growth advantage in presence of Fe(3+): ferrichrome as iron source. Rajendran, G., Mistry, S., Desai, A.J., Archana, G. Arch. Microbiol. (2007) [Pubmed]
  4. The FhuA protein is involved in microcin 25 uptake. Salomón, R.A., Farías, R.N. J. Bacteriol. (1993) [Pubmed]
  5. Protein fusions of beta-galactosidase to the ferrichrome-iron receptor of Escherichia coli K-12. Coulton, J.W., Mason, P., Cameron, D.R., Carmel, G., Jean, R., Rode, H.N. J. Bacteriol. (1986) [Pubmed]
  6. Cloning and expression of the fhu genes involved in iron(III)-hydroxamate uptake by Escherichia coli. Fecker, L., Braun, V. J. Bacteriol. (1983) [Pubmed]
  7. The fhu genes of Rhizobium leguminosarum, specifying siderophore uptake proteins: fhuDCB are adjacent to a pseudogene version of fhuA. Stevens, J.B., Carter, R.A., Hussain, H., Carson, K.C., Dilworth, M.J., Johnston, A.W. Microbiology (Reading, Engl.) (1999) [Pubmed]
  8. Cloning and characterization of a Campylobacter jejuni iron-uptake operon. Galindo, M.A., Day, W.A., Raphael, B.H., Joens, L.A. Curr. Microbiol. (2001) [Pubmed]
  9. Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. Hantke, K. Mol. Gen. Genet. (1981) [Pubmed]
  10. Transport of iron across the outer membrane. Braun, V., Günter, K., Hantke, K. Biology of metals. (1991) [Pubmed]
  11. Plasmid and chromosomal mutants in the iron(III)-aerobactin transport system of Escherichia coli. Use of streptonigrin for selection. Braun, V., Gross, R., Köster, W., Zimmermann, L. Mol. Gen. Genet. (1983) [Pubmed]
  12. The ferrichrome-iron receptor of Escherichia coli K-12. Antigenicity of the fhuA protein. Coulton, J.W. Biochim. Biophys. Acta (1982) [Pubmed]
 
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