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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Fernández‐Otal, Á., Guío, J., Sarasa‐Buisan, C., Peleato, M. L., Fillat, M. F., Lanas, Á., & Bes, M. T. (2024) · FEBS Journal · doi:10.1111/febs.17156 · Cited by 2
“We used divalent metal Mn 2 + as a surrogate for Fe 2 + for the in vitro analyses of Fur homolog because ferrous iron readily oxidizes to Fe 3 + in air [49].”
Siderophore alcaligin E production by Alcaligenes eutrophus CH34: features of the ale-operon and application perspectives of alcaligin E for leaching of heavy metals
Gilis, A., Khan, M. A., Verrijdt, W., Taghavi, S., Diels, L., Mergeay, M., & van der Lelie, D. (1997) · Springer eBooks · doi:10.1007/978-94-017-1711-3_6 · Cited by 2
Characterization of the siderophore transport protein AsbJ in Aeromonas salmonicida subsp. salmonicida
Najimi, M. (2011) · Comparative Clinical Pathology · doi:10.1007/s00580-011-1292-6 · Cited by 2
Transcriptional regulation of the ferric aerobactin receptor gene by a GntR-like repressor IutR in Vibrio furnissii
Tanabe, T., Isshiki, A., Miyamoto, K., Tsujibo, H., Yamamoto, S., & Funahashi, T. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny220 · Cited by 2
Cloning and Characterization of a fur Homologue from Azospirillum brasilense Sp7
Alahari, A., Tripathi, A. K., & Rudulier, D. L. (2006) · Current Microbiology · doi:10.1007/s00284-005-0204-x · Cited by 2
“The promoters of Fur-repressed genes contain one or two target DNA sequences called iron boxes, displaying various degrees of similarity to the 19-bp palindromic consensus 5¢-GATAATGATAATCATTATC-3¢ sequence [6, 8, 9].”
Background
Sensing Metals: the Versatility of Fur
Cha, S., Shin, J., & Roe, J. (2014) · ASM Press eBooks · doi:10.1128/9781555816841.ch12 · Cited by 2
Interactions of heme and other metal ion complexes with the bacterial Fe‐uptake regulatory protein and with bacterioferritin
Spiro, S., Kilic, M. A., Lewin, A. C., Dobbin‐Namiranian, S., THOMSON, A. J., & Moore, G. R. (1999) · Wiley eBooks · doi:10.1002/9783527613700.ch14 · Cited by 2
Fur‐Independent Induction of Helicobacter pylori Flavodoxin‐Encoding Gene (fldA) Under Iron Starvation
Kwon, D. H., & Versalovic, J. A. (2009) · Helicobacter · doi:10.1111/j.1523-5378.2009.00669.x · Cited by 2
REGULATION OF MNSOD IN E.COLI IN RESPONSE TO ENVIRONMENTAL STIMULI.
Touati, D., Tardat, B., & Compan, I. (1991) · Elsevier eBooks · doi:10.1016/b978-0-08-041749-3.50009-7 · Cited by 2
Isolation and Identification of Fur Binding Genes in Escherichia coli
Oh, M., Chai, S.-H., & Wee, S. (1999) · Molecules and Cells · doi:10.1016/s1016-8478(23)13579-5 · Cited by 2
Self-citation
Regulation of Oxidative Stress–Related Genes Implicated in the Establishment of Opportunistic Infections byBacteroides Fragilis
Teixeira, F. L., Domingues, R. M. C. P., & Lobo, L. A. (2016) · doi:10.1002/9781119004813.ch57 · Cited by 2
The Shiga Toxin Family: Molecular Nature and Possible Role in Disease
BRUNTON, J. L. (1990) · Elsevier eBooks · doi:10.1016/b978-0-12-370390-3.50021-4 · Cited by 2
Iron Scavenging in the Pathogenesis of Escherichia coli
WILLIAMS, P. H., & Roberts, M. (1989) · Elsevier eBooks · doi:10.1016/b978-0-12-355574-8.50025-2 · Cited by 2
Iron Scavenging in the Pathogenesis of Escherichia coli
WILLIAMS, P. H., & ROBERTS, M. (1989) · Elsevier eBooks · doi:10.1016/b978-0-12-355575-5.50024-1 · Cited by 2
Aerobactin: A Multifaceted Siderophore
Ghosh, S. (2025) · Indian Journal of Microbiology · doi:10.1007/s12088-025-01509-5 · Cited by 1
Norepinephrine derepresses the Fur regulon of Neisseria gonorrhoeae to enable growth in iron-limited conditions
Westlake, C. S., Stoudenmire, J. L., Bhatia, I., Perera, Y. R., Krueger, R. M., Cornelissen, C. N., Chazin, W., Kendall, M. M., & Criss, A. K. (2026) · Journal of Bacteriology · doi:10.1128/jb.00597-25 · Cited by 1
Iron-regulated phenylalanyl-tRNA synthetase activity in Azotobacter vinelandii
Page, W. J., Mehrotra, M., Woestyne, M. V., Tindale, A. E., Choy, S. L. K., Macyk, A. S., & Leskiw, B. K. (2003) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(02)01067-4 · Cited by 1
Comparative genomics reveals ‘novel’ Fur regulated sRNAs and coding genes in diverse proteobacteria
Sridhar, J., Sabarinathan, R., Gunasekaran, P., & Sekar, K. (2012) · Gene · doi:10.1016/j.gene.2012.12.057 · Cited by 1
Effect of the amino acid substitution in the DNA-binding domain of the Fur regulator on production of pyoverdine
Valešová, R., Palyzová, A., Marešová, H., Štěpánek, V., Babiak, P., & Kyslı́k, P. (2012) · Folia Microbiologica · doi:10.1007/s12223-012-0210-x · Cited by 1
“The C-terminal domain serves also for dimerization of the Fur and is required for the interactions of the repressor with DNA: the Fur repressor assembles immediately into a dimer (Coy and Neilands 1991) and, in the presence of Fe(II), the dimer binds to DNA palindrome, a Fur box with GATAATGATAATCATTATC consensus sequ…”
Background
The chemical biology of siderophores from the bacterial endosymbiots of shipworms
Han, A. (2011) · doi:10.6083/m4g73bq8 · Cited by 1
Iron Deprivation: Physiology and Gene Regulation
Straus, N. A. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-48205-3_25 · Cited by 1
Regulation of Ferritin Synthesis and Degradation in Plants
Briat, J., & Lobréaux, S. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5993-1_16 · Cited by 1
Acid Adaptive Mechanisms of Campylobacter jejuni in the Gastrointestinal Tract
Askoura, M. (2015) · uO Research (University of Ottawa) · doi:10.20381/ruor-2806 · Cited by 1
“Under iron-enriched environments, Fur binds to Fe and the Fur-Fe complex binds to a DNA sequence known as the Fur-box in the promoters of target genes (16, 17, 90, 107).”
REGULATION OF EXPRESSION OF A Neisseria gonorrhoeae tRNA-MODIFICATION ENZYME (Gcp)
Hernández, D. R. (2012) · UA Campus Repository (The University of Arizona) · Cited by 1
Mechanism and regulation of magnetosomal iron uptake and biomineralization in magnetospirillum gryphiswaldense
Uebe, R. (2012) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.15344 · Cited by 1
Interplay Between O 2 and Iron in Gene Expression: Environmental Sensing by FNR, ArcA, and Fur in Bacteria
Troxell, B., & Hassan, H. M. (2016) · Wiley eBooks · doi:10.1002/9781119004813.ch105 · Cited by 1
Molecular Biology and Regulation of Iron Acquisition by Escherichia coli K12
Neilands, J. B. (1990) · Elsevier eBooks · doi:10.1016/b978-0-12-370390-3.50013-5 · Cited by 1
Self-citation
The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn2+ and Co2+ to EC Fur dimer-DNA ComplexPreprint
Hamed, M. Y., & Jabour, S. (2020) · Preprints.org · doi:10.20944/preprints202011.0146.v2
The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn2+ and Co2+ to EC Fur dimer-DNA ComplexPreprint
Hamed, M. Y., & Jabour, S. (2020) · Preprints.org · doi:10.20944/preprints202011.0146.v3
The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn2+ and Co2+ to EC Fur dimer-DNA ComplexPreprint
Hamed, M. Y., & Jabour, S. (2020) · Preprints.org · doi:10.20944/preprints202011.0146.v4
The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn2+ and Co2+ to EC Fur dimer-DNA ComplexPreprint
Hamed, M. Y. (2020) · Preprints.org · doi:10.20944/preprints202011.0146.v1
“Experimentally, Fe, Co [7] and Mn acted as corepressors to activate Fur binding to the DNA[2] while Zn, Fe, Cd failed to activate Fur binding[2][8].”
BackgroundMethod
Iron acquisition from transferrins by Campylobacter jejuni
Miller, C. E. (2009) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 1

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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