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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Background
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Background
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Comparison of Highly and Weakly Virulent Dickeya solani Strains, With a View on the Pangenome and Panregulon of This Species
Golanowska, M., Potrykus, M., Motyka‐Pomagruk, A., Kabza, M., Bacci, G., Galardini, M., Bazzicalupo, M., Makałowska, I., Smalla, K., Mengoni, A., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01940 · Cited by 42
“Regulon predictions were conducted on the basis of experimentally established and previously described sequences of the binding sites for four TFs: KdgR, Fur, CRP, and PecS (de Lorenzo et al., 1987; Sauvage et al., 1996; Rodionov et al., 2004; Rouanet et al., 2004; Franza et al., 2005).”
Background
Siderophore-mediated iron uptake in Alcaligenes eutrophus CH34 and identification of aleB encoding the ferric iron-alcaligin E receptor
Gilis, A., Khan, M. A., Cornélis, P., Meyer, J., Mergeay, M., & van der Lelie, D. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.18.5499-5507.1996 · Cited by 42
“No sequence resembling the iron box consensus sequence (13) was found.”
Background
Deletion of the Ferric Uptake Regulator Fur Impairs the In Vitro Growth and Virulence of Actinobacillus pleuropneumoniae
Jacobsen, I. D., Gerstenberger, J., Gruber, A. D., Bossé, J. T., Langford, P. R., Hennig‐Pauka, I., Meens, J., & Gerlach, G.-F. (2005) · Infection and Immunity · doi:10.1128/iai.73.6.3740-3744.2005 · Cited by 42
Genetics and regulation of enterobactin genes in Shigella flexneri
Schmitt, M. P., & Payne, S. M. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.12.5579-5587.1988 · Cited by 42
An anti‐repression Fur operator upstream of the promoter is required for iron‐mediated transcriptional autoregulation in Helicobacter pylori
Delany, I., Spohn, G., Rappuoli, R., & Scarlato, V. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03757.x · Cited by 40
Iron‐responsive gene expression in Pseudomonas fluorescens M114; cloning and characterization of a transcription‐activating factor, PbrA
Sexton, R., Gill, P. R., Callanan, M. J., O’Sullivan, D. J., Dowling, D. N., & O’Gara, F. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.tb02244.x · Cited by 41
An Escherichia coli enterobactin cluster gene with sequence homology to trpE and pabB
Elkins, M. F., & Earhart, C. F. (1988) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1988.tb03146.x · Cited by 41
Comparative genomic analysis and characterization of incompatibility group FIB plasmid encoded virulence factors of Salmonella enterica isolated from food sources
Khajanchi, B. K., Hasan, N. A., Choi, S. Y., Han, J., Zhao, S., Colwell, R. R., Cerniglia, C. E., & Foley, S. L. (2017) · BMC Genomics · doi:10.1186/s12864-017-3954-5 · Cited by 42
“Fur binds to consensus regions upstream of target genes Fur-box [47, 48].”
Background
Understanding and engineering electrochemically active bacteria for sustainable biotechnology
Hirose, A., Kasai, T., Koga, R., Suzuki, Y., Kouzuma, A., & Watanabe, K. (2019) · Bioresources and Bioprocessing · doi:10.1186/s40643-019-0245-9 · Cited by 39
Characterization of a Vibrio vulnificus LysR homologue, HupR, which regulates expression of the haem uptake outer membrane protein, HupA
Litwin, C. M., & Quackenbush, J. (2001) · Microbial Pathogenesis · doi:10.1006/mpat.2001.0472 · Cited by 41
Identification of Siderophore Biosynthesis Genes Essential for Growth of Aeromonas salmonicida under Iron Limitation Conditions
Najimi, M., Lemos, M. L., & Osorio, C. R. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02728-07 · Cited by 40
Growth and siderophores production in Alcaligenes faecalis is regulated by metal ions
Sayyed, R. Z., & Chincholkar, S. B. (2010) · Indian Journal of Microbiology · doi:10.1007/s12088-010-0021-1 · Cited by 40
Immunogenicity of iron-regulated outer membrane proteins of Pasteurella multocida A:3 in cattle: molecular characterization of the immunodominant heme acquisition system receptor (HasR) protein
Prado, M. E., Dabo, S. M., & Confer, A. W. (2005) · Veterinary Microbiology · doi:10.1016/j.vetmic.2004.11.009 · Cited by 39
Binding of the ferric uptake regulation repressor protein (Fur) to Mn(II), Fe(II), Co(II), and Cu(II) ions as co-repressors: electronic absorption, equilibrium, and 57Fe Mossbauer studies
Hamed, M. Y., Neilands, J. B., & Huynh, V. (1993) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(93)80025-5 · Cited by 38
Self-citation
The fur gene from Klebsiella pneumoniae: characterization, genomic organization and phylogenetic analysis
Achenbach, L. A., & Yang, W. (1997) · Gene · doi:10.1016/s0378-1119(96)00642-7 · Cited by 36
Ferric Uptake Regulator (FUR) protein: properties and implications in cyanobacteria
Kaushik, M. S., Singh, P. K., Tiwari, B., & Mishra, A. K. (2015) · Annals of Microbiology · doi:10.1007/s13213-015-1134-x · Cited by 38
“…general a 17–21 kDa polypeptide (Bagg and Neilands 1987; Saito et al. 1991; Martin-Luna et al. 2005) that acts as an iron-dependent transcriptional regulator that regulates the expression of several iron responsive genes (Bagg and Neilands 1987; de Lorenzo et al. 1987; Escolar et al. 1997, 1998).”
Transcript analysis of nrrF, a Fur repressed sRNA of Neisseria gonorrhoeae
Ducey, T. F., Jackson, L. A., Orvis, J., & Dyer, D. W. (2009) · Microbial Pathogenesis · doi:10.1016/j.micpath.2008.12.003 · Cited by 38
Vibrio fischeri siderophore production drives competitive exclusion during dual‐species growth
Eickhoff, M. J., & Bassler, B. L. (2020) · Molecular Microbiology · doi:10.1111/mmi.14509 · Cited by 34
“Aerobactin production is Fur-regulated in E. coli (de Lorenzo et al., 1987), and Fur boxes have been identified neighboring the aerobactin biosynthetic genes in V. hollisae (Suzuki et al., 2006).”
Background
TonB of Escherichia coli activates FhuA through interaction with the β-barrel a aThe GenBank accession number for the sequence reported in this paper is Y15319.
Killmann, H., Herrmann, C., Torun, A., Jung, G., & Braun, V. (2002) · Microbiology · doi:10.1099/00221287-148-11-3497 · Cited by 38
IscR Regulation of Capsular Polysaccharide Biosynthesis and Iron-Acquisition Systems in Klebsiella pneumoniae CG43
Wu, C.-C., Wang, C., Chen, Y., Lin, T., Jinn, T., & Lin, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107812 · Cited by 38
Members of the Fur protein family regulate iron and zinc transport in E. coli and characteristics of the Fur-regulated fhuF protein.
Hantke, K. (2002) · PubMed · Cited by 38
Heme Utilization in Bordetella avium Is Regulated by RhuI, a Heme-Responsive Extracytoplasmic Function Sigma Factor
Kirby, A. E., Metzger, D. J., Murphy, E. R., & Connell, J. W. (2001) · Infection and Immunity · doi:10.1128/iai.69.11.6951-6961.2001 · Cited by 38
“coli consensus Fur box (7) was identified (8 of 19 nucleotides) (Fig.”
Background
Isolation and characterization of Bordetella bronchiseptica mutants deficient in siderophore activity
Armstrong, S. K., & Clements, M. O. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.4.1144-1152.1993 · Cited by 38
“coli is primarily mediated by the Fur repressor protein and is maximal during iron stress and repressed under iron-replete conditions (4, 7, 14).”
Background
Involvement of the FtsH (HflB) protease in the activity of σ54 promoters
Carmona, M., & de Lorenzo, V. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01169.x · Cited by 38
“To verify that the loss of FtsH did not affect the reporter enzyme (b-galactosidase), we transformed the same isogenic ftsH þ/ftsH ¹ strains with plasmid pCON1 (Table 1), which bears a lacZ fusion to the s70 promoter of the aerobactin operon of E. coli (de Lorenzo et al., 1987).”
Background
Electrospray ionization mass spectrometry analysis of the apo‐ and metal‐substituted forms of the Fur protein
Michaud‐Soret, I., Adrait, A., Jaquinod, M., Forest, É., Touati, D., & Latour, J. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00963-0 · Cited by 38
Regulation of the expression of bacterial iron transport genes: possible role of an antisense RNA as a repressor
Salinas, P. C., Waldbeser, L. S., & Crosa, J. H. (1993) · Gene · doi:10.1016/0378-1119(93)90535-b · Cited by 37
Analysis of Fur binding to operator sequences within the Neisseria gonorrhoeae fbpA promoter
Desai, P. J., Angerer, A., & Genco, C. A. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.16.5020-5023.1996 · Cited by 37
“DNase I footprinting experiments were essentially carried out as previously described (6), with slight modifications, with the DNaseI footprinting system (BRL, Life Technologies, Inc.”
BackgroundMethod
Identification of Differentially Regulated Francisella tularensis Genes by Use of a Newly Developed Tn 5 -Based Transposon Delivery System
Buchan, B. W., McLendon, M. K., & Jones, B. D. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02882-07 · Cited by 37
“Ferrous iron binds to Fur as a corepressor, causing an allosteric change in the protein that results in Fur binding to conserved nucleotide sequences which often overlap the promoter regions of Fur-regulated genes (13, 16).”
Background
Fur Activates Expression of the 2-Oxoglutarate Oxidoreductase Genes ( oorDABC ) in Helicobacter pylori
Gilbreath, J. J., West, A. L., Pich, Ò. Q., Carpenter, B. M., Michel, S. L. J., & Merrell, D. S. (2012) · Journal of Bacteriology · doi:10.1128/jb.01226-12 · Cited by 36
“This binding physically prevents the RNA polymerase (RNAP) from interacting with the promoter and initiating transcription (2, 14, 16, 18, 27).”
Background
Characterization and optimization of siderophore production from Pseudomonas fluorescens strain isolated from sugarcane rhizosphere.
Tailor, A. J., Joshi, B. H., Bhakta, C. G., & Vidyanagar, G. (2012) · Journal of environmental research and development/Journal of Environment Research and Development · Cited by 36
The Bradyrhizobium japonicum fegA gene encodes an iron-regulated outer membrane protein with similarity to hydroxamate-type siderophore receptors
LeVier, K., & Guerinot, M. L. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.24.7265-7275.1996 · Cited by 36
A Single Nucleotide Change Affects Fur-Dependent Regulation of sodB in H. pylori
Carpenter, B. M., Gancz, H., Gonzalez‐Nieves, R., West, A. L., Whitmire, J. M., Michel, S. L. J., & Merrell, D. S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005369 · Cited by 35
Biosynthetic and regulatory elements involved in the production of the siderophore vanchrobactin in Vibrio anguillarum
Balado, M., Osorio, C. R., & Lemos, M. L. (2008) · Microbiology · doi:10.1099/mic.0.2008/016618-0 · Cited by 35
Transcriptional responses of Escherichia coli during recovery from inorganic or organic mercury exposure
LaVoie, S. P., & Summers, A. O. (2018) · BMC Genomics · doi:10.1186/s12864-017-4413-z · Cited by 35
“Fur can also bind other divalent metals [108], so Hg(II)-Fur might mimic Fe-Fur as an iron uptake repressor under these conditions to limit Fenton-mediated damage from excess iron.”
Background
Characterization of the Interaction between Fur and the Iron Transport Promoter of the Virulence Plasmid in Vibrio anguillarum
Chai, S., Welch, T. J., & Crosa, J. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33841 · Cited by 35
Characterization of the DNA- and Metal-Binding Properties of Vibrio anguillarum Fur Reveals Conservation of a Structural Zn 2+ Ion
Heldwein, E. E. Z., Crosa, J. H., & Brennan, R. G. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.21.6264-6267.2000 · Cited by 34
“To date, the most extensive biochemical studies have been limited to the Escherichia coli Fur protein, which in the presence of various divalent metals that act as corepressors binds a conserved 19-bp operator sequence, the iron box, which is located in the promoter region of iron uptake genes (4, 5, 9).”
BackgroundInfluential

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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