Cited by 536Bacterial Genetics and BiotechnologyEscherichia coli research studiesIron Metabolism and Disorders

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Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor

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de Lorenzo, V, Wee, S, Herrero, M, Neilands, J B·1987·Journal of Bacteriology

DOI 10.1128/jb.169.6.2624-2630.1987PMC PMC212138

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Abstract

The promoter region of the pColV-K30-encoded operon specifying biosynthesis and transport of the siderophore aerobactin was subjected to deletion analysis to determine the smallest DNA sequence affording iron regulation of a iucA'-'lacZ gene fusion. A 78-base-pair (bp) region containing the main (P1) promoter retained the character of inducibility under iron starvation. A 250-bp fragment carrying this sequence was examined for protection against DNase I by the Fur protein, the product of a gene (fur) required for negative control of several iron-regulated functions. The DNase I footprints, in the presence of various divalent heavy-metal ions added as corepressors, revealed two contiguous binding sites with different lengths and affinities for Fur. Increased concentrations of the protein appeared to elicit formation of repressor oligomers which bind to the upstream and downstream regions of the P1 promoter in a metal-dependent fashion, but with a presently undefined stoichiometry. The primary site for Fur binding spans 31 bp and contains two overlapping symmetry dyads which share the sequence 5'-TCATT-3'. It also contains extensive homology with a 19-bp consensus sequence for iron-regulated genes as deduced from comparison with the fhuA and fepA putative promoter sequences.

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A SitABCD homologue from an avian pathogenic Escherichia coli strain mediates transport of iron and manganese and resistance to hydrogen peroxide
Sabri, M., Léveillé, S., & Dozois, C. M. (2006) · Microbiology · doi:10.1099/mic.0.28682-0 · Cited by 162
“The predicted Fur- and MntR-binding regions were derived from the consensus sequences described by de Lorenzo et al. (1987) and Patzer & Hantke (2001) respectively, and are also conserved in PsitABCD of E. coli CFT073 and in Sh. flexneri strains (data not shown; Runyen-Janecky et al., 2003).”
Method
Dual Repression by Fe 2+ -Fur and Mn 2+ -MntR of the mntH Gene, Encoding an NRAMP-Like Mn 2+ Transporter in Escherichia coli
Patzer, S. I., & Hantke, K. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.16.4806-4813.2001 · Cited by 160
“The binding site GAgAATG ATtATCAaatTC matches the Fur-box consensus sequence GATAATGATAATCATTATC (9) in 14 of 19 nt (mismatches are shown as lowercase letters).”
Background
Legionella pneumophila feoAB Promotes Ferrous Iron Uptake and Intracellular Infection
Robey, M., & Cianciotto, N. P. (2002) · Infection and Immunity · doi:10.1128/iai.70.10.5659-5669.2002 · Cited by 160
“coli counterpart, is subject to regulation by bacterial intracellular Fe(2) levels (15).”
Colicin V virulence plasmids
Waters, V. L., & Crosa, J. H. (1991) · Microbiological Reviews · doi:10.1128/mmbr.55.3.437-450.1991 · Cited by 159
“terized the aerobactin systems operon (9, 13, 17, 27, 29, 52) and the flanking genetic regions (66, 85-87, 114) in terms of genetic structure, function, and regulation.”
Background
Identification of novel cis‐acting elements, IDE1 and IDE2, of the barley IDS2 gene promoter conferring iron‐deficiency‐inducible, root‐specific expression in heterogeneous tobacco plants
Kobayashi, T., Nakayama, Y., Itai, R. N., Nakanishi, H., Yoshihara, T., Mori, S., & Nishizawa, N. K. (2003) · The Plant Journal · doi:10.1046/j.1365-313x.2003.01920.x · Cited by 156
W ITHHOLDING AND E XCHANGING I RON : Interactions Between Erwinia spp. and Their Plant Hosts
Expert, D. (1999) · Annual Review of Phytopathology · doi:10.1146/annurev.phyto.37.1.307 · Cited by 159
Structural dynamics and functional domains of the Fur protein
Coy, M., & Neilands, J. B. (1991) · Biochemistry · doi:10.1021/bi00247a016 · Cited by 154
Self-citation
Identification of a new iron regulated locus of Salmonella typhi
Bäumler, A. J., Tsolis, R. M., van der Velden, A. W. M., Stojiljković, I., Anic, S., & Heffron, F. (1996) · Gene · doi:10.1016/s0378-1119(96)00560-4 · Cited by 155
The Bacterial Irr Protein Is Required for Coordination of Heme Biosynthesis with Iron Availability
Hamza, I., Chauhan, S., Hassett, R. F., & O’Brian, M. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.21669 · Cited by 154
Effect of Salmonella typhimurium ferric uptake regulator (fur) mutations on iron- and pH-regulated protein synthesis
Foster, J. W., & Hall, H. K. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.13.4317-4323.1992 · Cited by 154
“For example, it will be useful to examine type C and D loci for the presence or absence of a Fur box, the identified consensus DNA sequence to which iron-complexed Fur binds (15).”
Method
Review
Creighton, T. (1997) · Biological Chemistry · doi:10.1515/bchm.1997.378.8.731 · Cited by 150
Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni
Pesci, E. C., Cottle, D. L., & Pickett, C. L. (1994) · Infection and Immunity · doi:10.1128/iai.62.7.2687-2694.1994 · Cited by 149
“jejuni sodB gene for sequences that resemble the Fur-binding consensus sequence (13).”
Background
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. (1999) · Biochemistry · doi:10.1021/bi982788s · Cited by 147
The ins and outs of siderophore mediated iron uptake by extra-intestinal pathogenic Escherichia coli
Garénaux, A., Caza, M., & Dozois, C. M. (2011) · Veterinary Microbiology · doi:10.1016/j.vetmic.2011.05.023 · Cited by 141
Dual Role of Desferrioxamine in Erwinia amylovora Pathogenicity
Dellagi, A., Brisset, M., Paulin, J. P., & Expert, D. (1998) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi.1998.11.8.734 · Cited by 141
FptA, the Fe(III)-pyochelin receptor of Pseudomonas aeruginosa: a phenolate siderophore receptor homologous to hydroxamate siderophore receptors
Ankenbauer, R. G., & Quan, H. N. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.2.307-319.1994 · Cited by 141
“This putative "iron box" in the fptA promoter, 5'-ATAATGATAAGCATTATC-3', matched the consensus Fur-binding site, 5'-ATAATGATAATCATTATC-3' (10, 20), at 17 of 18 positions.”
Background
Gene Expression in Pseudomonas aeruginosa : Evidence of Iron Override Effects on Quorum Sensing and Biofilm-Specific Gene Regulation
Bollinger, N., Hassett, D. J., Iglewski, B. H., Costerton, J. W., & McDermott, T. R. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.6.1990-1996.2001 · Cited by 139
“The Fe(II)-Fur complex directly binds to the promoter region of genes that contain a specific regulatory sequence known as the iron box (9).”
Background
Iron-regulated outer membrane proteins of Escherichia coli K-12 and mechanism of action of catechol-substituted cephalosporins
Curtis, N. A. C., Eisenstadt, R. L., East, S. J., Cornford, R. J., Walker, L., & White, A. J. (1988) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.32.12.1879 · Cited by 137
“and extends to the expression of aerobactin biosynthetic and uptake genes carried by certain ColV plasmids (1, 4, 9, 47).”
Background
Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa
Visca, P., Ciervo, A., & Orsi, N. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.4.1128-1140.1994 · Cited by 137
Identification and cloning of a fur regulatory gene in Yersinia pestis
Staggs, T. M., & Perry, R. D. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.2.417-425.1991 · Cited by 136
“Aerobactin- (16, 38), enterobactin- (38, 45), ferni-”
Role for the outer membrane ferric siderophore receptor PupB in signal transduction across the bacterial cell envelope.
Koster, M. C., van Klompenburg, W., Bitter, W., Leong, J., & Weisbeek, P. J. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06574.x · Cited by 134
Transcriptomic and Proteomic Characterization of the Fur Modulon in the Metal-Reducing Bacterium Shewanella oneidensis
Wan, X., VerBerkmoes, N. C., McCue, L. A., Stanek, D., Connelly, H. M., Hauser, L., Wu, L., Liu, X., Yan, T., Leaphart, A. B., et al. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.24.8385-8400.2004 · Cited by 132
Novel two-component transmembrane transcription control: regulation of iron dicitrate transport in Escherichia coli K-12
Hove, B. V., Staudenmaier, H., & Braun, V. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.12.6749-6758.1990 · Cited by 132
“Fur repression seems also to include the fecI and fecR regulatory genes, since a region upstream of fec! exhibits 78 or 73% homology to the consensus sequence of the DNA-binding site of the Fur iron repressor (7, 9, 32, 39).”
Background
Identification and transcriptional organization of a gene cluster involved in biosynthesis and transport of acinetobactin, a siderophore produced by Acinetobacter baumannii ATCC 19606T
Mihara, K., Tanabe, T., Yamakawa, Y., Funahashi, T., Nakao, H., Narimatsu, S., & Yamamoto, S. (2004) · Microbiology · doi:10.1099/mic.0.27141-0 · Cited by 131
Structure of the Shigella dysenteriae haem transport locus and its phylogenetic distribution in enteric bacteria
Wyckoff, E. E., Duncan, D., Torres, A. G., Mills, M., Maase, K., & Payne, S. M. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00873.x · Cited by 131
“Although this region does not contain any obvious 110 and 135 promoter elements, it does contain a sequence (GAT ATT TCGGGGC ATT TAT) with homology to the consensus Fur box (deLorenzo et al., 1987; Griggs and Konisky, 1989).”
Background
Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other peripiasmic binding protein‐dependent systems in Escherichia coli
Shea, C., & McIntosh, M. A. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb00788.x · Cited by 129
The structure of the Helicobacter pylori ferric uptake regulator Fur reveals three functional metal binding sites
Dian, C., Vitale, S., Leonard, G. A., Bahlawane, C., Fauquant, C., Leduc, D., Muller, C., Reuse, H. D., Michaud‐Soret, I., & Terradot, L. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07517.x · Cited by 127
“Molecular Microbiology (2011) 79(5), 1260–1275 doi:10.1111/j.1365-2958.2010.07517.x First published online 5 January 2011 © 2011 Blackwell Publishing Ltd called ‘Fur boxes’, repressing expression of genes involved in iron uptake (Bagg and Neilands, 1987; de Lorenzo et al., 1987; 1988).”
BackgroundInfluential
Fur regulon of Salmonella typhimurium: identification of new iron-regulated genes
Tsolis, R. M., Bäumler, A. J., Stojiljković, I., & Heffron, F. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.16.4628-4637.1995 · Cited by 127
Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co‐ordination
Sheikh, M. A., & Taylor, G. L. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06718.x · Cited by 126
“As reported for other Fur proteins, VcFur shares the ability to bind DNA in the presence of different metals (Bagg and Neilands, 1987; de Lorenzo et al., 1987).”
Background
Characterization of the Vibrio cholerae outer membrane heme transport protein HutA: sequence of the gene, regulation of expression, and homology to the family of TonB-dependent proteins
Henderson, D. P., & Payne, S. M. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.11.3269-3277.1994 · Cited by 125
“Under conditions of iron sufficiency, Fur binds to a highly conserved region called the Fur box upstream of iron-regulated genes and blocks transcription (1, 7, 15).”
Background
PrhA controls a novel regulatory pathway required for the specific induction of Ralstonia solanacearum hrp genes in the presence of plant cells
Marenda, M. S., Brito, B., Callard, D., Genin, S., Barberis, P. A., Boucher, C. A., & Arlat, M. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00692.x · Cited by 121
“…receptor genes are regulated by the Fur protein, which binds to specific DNA sequences in the presence of Fe2þ, the so called ‘Fur-box’, located within the operator of iron-regulated promoters and thus ensures transcriptional repression in iron-replete conditions (de Lorenzo et al., 1987).”
Background
Identification and Characterization of Genes Required for Biosynthesis and Transport of the Siderophore Vibrioferrin in Vibrio parahaemolyticus
Tanabe, T., Funahashi, T., Nakao, H., Miyoshi, S.-I., Shinoda, S., & Yamamoto, S. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.23.6938-6949.2003 · Cited by 128
“Fur complexed with Fe(2) binds to DNA with a 19-bp consensus palindromic sequence, called the Fur box, within the promoter regions of iron uptake genes (2, 12), so that transcription of the genes is shut off, thus limiting the entry of excess iron into the cell.”
Background
X-ray Absorption Spectroscopy of a New Zinc Site in the Fur Protein fromEscherichia coli
Jacquamet, L., Aberdam, D., Adrait, A., Hazemann, J., Latour, J., & Michaud‐Soret, I. (1998) · Biochemistry · doi:10.1021/bi9721344 · Cited by 119
Recognition of DNA by Three Ferric Uptake Regulator (Fur) Homologs inBacillus subtilis
Fuangthong, M., & Helmann, J. D. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.21.6348-6357.2003 · Cited by 117
“The classical Fur box is a 19-bp (9-1-9) inverted repeat, GATAATGATAATCATTATC (13).”
Background
Manganese regulates expression of manganese peroxidase by Phanerochaete chrysosporium
Brown, J. A., Glenn, J. K., & Gold, M. H. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.6.3125-3130.1990 · Cited by 118
Nucleotide sequence of Escherichia coli isochorismate synthetase gene entC and evolutionary relationship of isochorismate synthetase and other chorismate-utilizing enzymes
Ozenberger, B. A., Brickman, T. J., & McIntosh, M. A. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.2.775-783.1989 · Cited by 118
Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator
Deng, Z., Wang, Q., Liu, Z., Zhang, M., Machado, A. C. D., Chiu, T.-P., Feng, C., Zhang, Q., Yu, L., Qi, L., et al. (2015) · Nature Communications · doi:10.1038/ncomms8642 · Cited by 117

Authors: de Lorenzo, V, Wee, S., Herrero, M., & Neilands, J. B.
Affiliations: University of California, Berkeley (US)
Venue: Journal of Bacteriology
Publisher: American Society for Microbiology
Published: 1987-06
Volume: 169
Issue: 6
Pages: 2624-2630
ISSN: 0021-9193 (ISSN-L)
1098-5530
DOI: 10.1128/jb.169.6.2624-2630.1987
PMC: PMC212138
OpenAlex: W2131282911
Cited by: 536
References: 22
Citations by year: 2026: 2 · 2025: 3 · 2024: 7 · 2023: 5 · 2022: 6 · 2021: 8 · 2020: 9 · 2019: 4 · 2018: 8 · 2017: 6 · 2016: 13 · 2015: 12 · 2014: 11 · 2013: 9 · 2012: 21
FWCI: 14.06
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Bacteriology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Ministerio de Economía y Competitividad
National Institutes of Health (1f05tw003577-01)
U.S. Public Health Service (A104156)
Fogarty International Center (1F05TWO3577-01-BI-5)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords: Fur repressor, iron regulation, promoter, DNase I footprinting, repressor binding sites, consensus sequence, siderophore biosynthesis, Escherichia coli
MeSH terms: Bacterial Proteins, Chromosome Deletion, Cloning, Molecular, Bacteriocin Plasmids, Escherichia coli, Gene Expression Regulation, Hydroxamic Acids, Iron, Operator Regions, Genetic, Operon, Promoter Regions, Genetic, Recombinant Fusion Proteins, Repressor Proteins, Transcription Factors

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Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor

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