The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
Open accessAbstract
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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“Consensus sequences bound by Fur in E. coli , P. aeruginosa , V. cholerae and C. jejuni are also AT rich 10 , 17 , 30 , 32 .”
From Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator (2015) · cites this paper as [32]
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Cloning, sequencing, and transcriptional regulation of the Vibrio cholerae fur gene
Litwin, C. M., Boyko, S. A., & Calderwood, S. B. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.6.1897-1903.1992 · Cited by 116
“A consensus DNA binding site for the Fur protein, consisting of a 21-bp dyad symmetric sequence, has been suggested (6, 7, 9, 11).”
BackgroundEsberg, B., Leung, H. E., Tsui, H. T., Björk, G. R., & Winkler, M. E. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.23.7256-7265.1999 · Cited by 114
“However, no putative Fur-binding site (16, 21) is present in the promoter of miaB.”
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“quence (18) upstream of the recently cloned and sequenced”
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Calderwood, S. B., & Mekalanos, J. J. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.2.1015-1017.1988 · Cited by 111
“The most conserved bases of the proposed consensus sequence for Fur binding are 5'-TCATT-3', which occur in complementary fashion in each half of the dyad repeat (3, 4).”
BackgroundProduction of microbial iron chelators (siderophores) by fluorescent Pseudomonads
Sayyed, R. Z., Badgujar, M. D., Sonawane, H. M., Mhaske, M. M., & Chincholkar, S. B. (2005) · Cited by 111
Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12
Andrews, S. C., Harrison, P. M., & Guest, J. R. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.7.3940-3947.1989 · Cited by 110
“A Fur-Fe2+ complex is thought to bind to a 19-bp recognition site known as the iron box in the operator regions of the regulated genes (8).”
BackgroundSchmitt, M. P., & Holmes, R. K. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.4.1141-1149.1994 · Cited by 108
“coli binds to a 19-bp inverted-repeat nucleotide sequence referred to as an iron box (7, 19).”
BackgroundKobayashi, T., Itai, R. N., Aung, M. S., Senoura, T., Nakanishi, H., & Nishizawa, N. K. (2011) · The Plant Journal · doi:10.1111/j.1365-313x.2011.04772.x · Cited by 111
“Under Fe starvation, Fe2+ is released from the Fur protein, which decreases the affinity of Fur to bind to DNA and derepresses downstream Fe acquisition-related genes (de Lorenzo et al., 1987).”
BackgroundGriggs, D. W., & Konisky, J. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.2.1048-1054.1989 · Cited by 106
“taining the cir promoter region was examined essentially by the method described previously to define operators in the aerobactin operon (12).”
BackgroundMethodInfluentialCharacterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum
Posey, J. E., Hardham, J. M., Norris, S. J., & Gherardini, F. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10887 · Cited by 105
Characterization of lbpA, the structural gene for a lactoferrin receptor in Neisseria gonorrhoeae
Biswas, G. D., & Sparling, P. F. (1995) · Infection and Immunity · doi:10.1128/iai.63.8.2958-2967.1995 · Cited by 106
“coli Fur box sequence gaT aAT gat aAt cAT Tat c (20) at four of seven conserved positions was located 88 bases upstream of the ribosome binding site.”
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Gray‐Owen, S. D., Loosmore, S. M., & Schryvers, A. B. (1995) · Infection and Immunity · doi:10.1128/iai.63.4.1201-1210.1995 · Cited by 102
“2, outlined sequence) shares 16 of 19 nt with the consensus ferric uptake regulator (Fur) proteinbinding site [GAT(AT)ATGAT(AT)AT(CT)ATTATC (10)].”
BackgroundRicci, S., Janulczyk, R., & Björck, L. (2002) · Infection and Immunity · doi:10.1128/iai.70.9.4968-4976.2002 · Cited by 95
Grant, K. A., & Park, S. F. (1995) · Microbiology · doi:10.1099/13500872-141-6-1369 · Cited by 97
Microbial Fungicides: Recent Approaches to Elucidating Mechanisms
Gutterson, N. I. (1990) · Critical Reviews in Biotechnology · doi:10.3109/07388559009038205 · Cited by 96
Brickman, T. J., Ozenberger, B. A., & McIntosh, M. A. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90229-f · Cited by 96
Fedhila, S., Daou, N., Lereclus, D., & Nielsen‐LeRoux, C. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05362.x · Cited by 95
“3), and highly similar to the Fur box consensus (5′- GATAATGA TAA TCATTATC-3′) (de Lorenzo et al., 1987).”
BackgroundTao, X., & Murphy, J. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36677-3 · Cited by 95
Iron assimilation storage in prokaryotes
Briat, J. (1992) · Journal of General Microbiology · doi:10.1099/00221287-138-12-2475 · Cited by 95
García, C. A., Alcaraz, E. S., Franco, M. A., & de Rossi, B. P. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00926 · Cited by 94
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Nandal, A., Huggins, C. C., Woodhall, M. R., McHugh, J. P., Rodríguez‐Quiñones, F., Quail, M. A., Guest, J. R., & Andrews, S. C. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06977.x · Cited by 93
“Since Fur is a transcriptional repressor utilizing ferrous iron as co-repressor (de Lorenzo et al., 1987; Escolar et al., 1997; 1998), it appears likely that the Fe2+–Fur complex transcriptionally activates ftnA by acting either directly or indirectly.”
BackgroundIdentification and cloning of a fur homolog from Neisseria gonorrhoeae
Berish, S. A., Subbarao, S., Chen, C. Y., Trees, D. L., & Morse, S. A. (1993) · Infection and Immunity · doi:10.1128/iai.61.11.4599-4606.1993 · Cited by 92
“has been the source of several biochemical studies (10, 14) suggesting that the N-terminal region of Fur interacts with DNA while the C-terminal region is involved in metal binding (10).”
BackgroundLin, C.-T., Wu, C.-C., Chen, Y.-S., Lai, Y.-C., Chi, C., Lin, J.-C., Chen, Y., & Peng, H.-L. (2011) · Microbiology · doi:10.1099/mic.0.044065-0 · Cited by 86
Webster, A., & Litwin, C. M. (2000) · Infection and Immunity · doi:10.1128/iai.68.2.526-534.2000 · Cited by 90
“coli show homology with this consensus sequence that ranges from 13 to 17 base pair matches (12, 13, 15, 17).”
BackgroundTranscriptional Regulation ofsitABCDofSalmonella entericaSerovar Typhimurium by MntR and Fur
Ikeda, J. S., Janakiraman, A., Kehres, D. G., Maguire, M. E., & Slauch, J. M. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.3.912-922.2005 · Cited by 90
Unification of the ferritin family of proteins.
Grossman, M. J., Hinton, S. M., Minak-Bernero, V., Slaughter, C. A., & Stiefel, E. I. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.6.2419 · Cited by 91
Henderson, N., Austin, S., & Dixon, R. A. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00334394 · Cited by 90
Fur regulates acid resistance in Shigella flexneri via RyhB and ydeP
Oglesby, A. G., Murphy, E. R., Iyer, V. R., & Payne, S. M. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04920.x · Cited by 90
Redox Sensing by Fe 2+ in Bacterial Fur Family Metalloregulators
Pinochet-Barros, A., & Helmann, J. D. (2018) · Antioxidants & Redox Signaling · doi:10.1089/ars.2017.7359 · Cited by 85
Discovery of Fur binding site clusters in Escherichia coli by information theory models
Chen, Z., Lewis, K. A., Shultzaberger, R. K., Lyakhov, I. G., Zheng, M., Doan, B., Storz, G., & Schneider, T. D. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm631 · Cited by 88
Zinc-dependent regulation of zinc import and export genes by Zur
Choi, S.-H., Lee, K.-L., Shin, J.-H., Cho, Y.-B., Cha, S., & Roe, J. (2017) · Nature Communications · doi:10.1038/ncomms15812 · Cited by 90
Litwin, C. M., & Calderwood, S. B. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.3.706-715.1993 · Cited by 89
“SM796 (fiur') pMLB1109 None 6 (1-15) 10 9 (1-23) pCML22 None 4,700 (2,300-7,200) 10 3,300 (2,100-5,500) pCML23 None 2,200 (1,700-2,800) 10 1,600 (1,400-1,700) SBC796 (fur) pMLB1109 None 11 (1-27) 10 11 (1-21) pCML22 None 3,100 (1,300-4,300) 10 3,300 (3,000-3,400) pCML23 None 1,600 (1,000-2,000) 10 1,000 (810-1,200)”
BackgroundSequence of the fhuE outer‐membrane receptor gene of Escherichia coli K12 and properties of mutants
Sauer, M., Hantke, K., & Braun, V. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb00609.x · Cited by 86
Bsat, N., & Helmann, J. D. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.14.4299-4307.1999 · Cited by 86
“In vitro studies have suggested that FurEC can be activated for DNA binding by several divalent ions, including Co(II), Cu(II), Cd(II), Fe(II), and Mn(II) (14).”
BackgroundHickey, E. K., & Cianciotto, N. P. (1997) · Infection and Immunity · doi:10.1128/iai.65.1.133-143.1997 · Cited by 88
“Most promoter regions of genes regulated by Fur contain at least one iron box (13, 20), generally occurring within the 235 region to the 210 region, that represents the binding site(s) for Fur-Fe(21) repressors (51).”
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Regulation of bacterial gene expression by metal–protein complexes
Hennecke, H. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb00538.x · Cited by 82
Brillard, J., Duchaud, É., Boemare, N. E., Kunst, F., & Givaudan, A. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.14.3871-3878.2002 · Cited by 84
“The identities with the 19-nucleotide sequence of the Fur-binding consensus sequence reported previously (18) are indicated below the sequence, with matches represented by “ ” and mismatches represented by “ ”; the total number of identities is indicated at the end.”
BackgroundTolmasky, M. E., Wertheimer, A. M., Actis, L. A., & Crosa, J. H. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.1.213-220.1994 · Cited by 83
“This operator consists of a 21-bp dyad symmetric consensus sequence (10, 11, 20-22).”
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“coli (7, 8, 11, 12) and to the dyad symmetric sequence located in the promoter region of itgA (15).”
BackgroundInfluentialHan, A., Sandy, M., Fishman, B., Silva, A. E. T., Soares, C. A. G., Distel, D. L., Butler, A., & Haygood, M. G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076151 · Cited by 81
“[46].”
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“uses Fe(II) as corepressor to bind to an operator region in the aerobactin promoter (4, 17).”
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Membrillo‐Hernández, J., Ioannidis, N. E., & Poole, R. K. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00154-8 · Cited by 79
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“the promoter regions of these genes, termed Fur boxes, and thereby inhibits gene expression under iron-replete conditions (3, 13).”
BackgroundHardham, J. M., Stamm, L. V., Porcella, S. F., Frye, J. G., Barnes, N. Y., Howell, J. K., Mueller, S. L., Radolf, J. D., Weinstock, G. M., & Norris, S. J. (1997) · Gene · doi:10.1016/s0378-1119(97)00234-5 · Cited by 78
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Lee, J. H., Wang, T., Ault, K., Liu, J., Schmitt, M. P., & Holmes, R. K. (1997) · Infection and Immunity · doi:10.1128/iai.65.10.4273-4280.1997 · Cited by 77
“They also bind to different 19-bp consensus core operator sequences, namely 59-GATAATGATAATCATTATC-39 for Fur (10, 21) and 59-TTAGGTTAGCCTAACCTAA-39 for DtxR (42, 52).”
BackgroundIron uptake and metabolism in the rhizobia/legume symbioses
Guerinot, M. L. (1991) · Springer eBooks · doi:10.1007/978-94-011-3294-7_29 · Cited by 77
Teixidó, L., Carrasco, B., Alonso, J. C., Barbé, J., & Campoy, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019711 · Cited by 75
Lagos, R., Baeza, M., Corsini, G., Hetz, C. A., Strahsburger, E., Castillo, J. A., Vergara, C., & Monasterio, O. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02630.x · Cited by 76
Ferric Enterochelin Transport in Yersinia enterocolitica : Molecular and Evolutionary Aspects
Schubert, S., Fischer, D., & Heesemann, J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.20.6387-6395.1999 · Cited by 75
“coli Fur-binding consensus sequence (FBS) was found (Table 2) (14).”
BackgroundAdrait, A., Jacquamet, L., Pape, L. L., de Peredo, A. G., Aberdam, D., Hazemann, J., Latour, J., & Michaud‐Soret, I. (1999) · Biochemistry · doi:10.1021/bi9823232 · Cited by 75
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“DNA–protein interactions were probed with DNase I as described by de Lorenzo et al. (1988a). To this end, the 250 bp EcoRI–BamHI DNA fragment from plasmid pCON6 (de Lorenzo et al.”
MethodIron uptake and metabolism in the rhizobia/legume symbioses
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Purification and characterization of the diphtheria toxin repressor.
Schmitt, M. P., Twiddy, E. M., & Holmes, R. K. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7576 · Cited by 74
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Roles of the EnvZ/OmpR Two-Component System and Porins in Iron Acquisition in Escherichia coli
Gerken, H. G., Vuong, P., Soparkar, K., & Misra, R. (2020) · mBio · doi:10.1128/mbio.01192-20 · Cited by 73
The Bordetella bhu Locus Is Required for Heme Iron Utilization
Vanderpool, C. K., & Armstrong, S. K. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.14.4278-4287.2001 · Cited by 73
“coli consensus Fur-binding DNA sequence (19, 24).”
Angerer, A., & Braun, V. (1998) · Archives of Microbiology · doi:10.1007/s002030050600 · Cited by 72
Beucher, M., & Sparling, P. F. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.8.2041-2049.1995 · Cited by 72
Fur regulation in Yersinia species
Staggs, T. M., & Perry, R. D. (1992) · Molecular Microbiology · doi:10.1111/j.1365-2958.1992.tb01427.x · Cited by 72
Wee, S., Neilands, J. B., Bittner, M. L., Hemming, B. C., Haymore, B. L., & Seetharam, R. (1988) · BioMetals · doi:10.1007/bf01128019 · Cited by 72
Self-citationIron Transport and Metabolism in Escherichia, Shigella, and Salmonella
Mey, A. R., Gómez-Garzón, C., & Payne, S. M. (2021) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0034-2020 · Cited by 70
“There are multiple, sometimes overlapping, binding sites for Fur upstream of some Fur-regulated genes, including ftnA (13) and the aerobactin operon (14).”
BackgroundOh, M. H., Lee, S. M., Lee, D. H., & Choi, S. H. (2009) · Infection and Immunity · doi:10.1128/iai.01006-08 · Cited by 69
“The assigned sequence for the Fur binding, GATAATG ATAATCATTATC, scored a 79% homology to the consensus Fur binding sequence (6).”
BackgroundUebe, R., Voigt, B., Schweder, T., Albrecht, D., Katzmann, E., Lang, C., Böttger, L. H., Matzanke, B. F., & Schüler, D. (2010) · Journal of Bacteriology · doi:10.1128/jb.00319-10 · Cited by 69
Cloning and sequencing of the Legionella pneumophila fur gene
Hickey, E. K., & Cianciotto, N. P. (1994) · Gene · doi:10.1016/0378-1119(94)90615-7 · Cited by 72
Kozlov, Y. V., Kabishev, A. A., Luk'ianov, E. V., & Bayev, A. A. (1988) · Gene · doi:10.1016/0378-1119(88)90398-8 · Cited by 71
Schmitt, M. P., & Holmes, R. K. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01679.x · Cited by 71
Hunt, M. D., Pettis, G. S., & McIntosh, M. A. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.13.3944-3955.1994 · Cited by 72
“A reasonable location might be the adjacent region within the fes-entF promoter that resembles the consensus iron box sequence (18) and appears to be the key element in iron regulation of the fes transcript as well.”
BackgroundMethodInfluentialIdentification and cloning of a fur homologue from Neisseria meningitidis
Thomas, C. E., & Sparlling, P. F. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb00350.x · Cited by 71
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Rhizobacterial salicylate production provokes headaches!
Bakker, P. A. H. M., Ran, L., & Mercado‐Blanco, J. (2014) · Plant and Soil · doi:10.1007/s11104-014-2102-0 · Cited by 73
“…aeruginosa PAO1 (Serino et al. 1995, 1997), is positively controlled by the PchR protein in the presence of pyochelin (Reimmann et al. 1998) and negatively by the Fur (Ferric Uptake Regulation) repressor (Bagg and Neilands 1987; de Lorenzo et al. 1987) in the presence of iron (Serino et al. 1997).”
BackgroundProteus mirabilis amino acid deaminase: cloning, nucleotide sequence, and characterization of aad
Massad, G., Zhao, H., & Mobley, H. L. T. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.20.5878-5883.1995 · Cited by 70
Hancock, V., Dahl, M., & Klemm, P. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00241-10 · Cited by 72
“Fur also binds and shows activation by other divalent metal ions, such as Co(II), Mn(II), Zn(II), Cd(II), and Cu(II) (2, 9).”
BackgroundImpact of Anaerobiosis on Expression of the Iron-Responsive Fur and RyhB Regulons
Beauchene, N. A., Myers, K. S., Chung, D., Park, D. M., Weisnicht, A. M., Keleş, S., & Kiley, P. J. (2015) · mBio · doi:10.1128/mbio.01947-15 · Cited by 69
Autoregulation of Helicobacter pylori Fur revealed by functional analysis of the iron‐binding site
Delany, I., Spohn, G., Pacheco, A. B. F., Ieva, R., Alaimo, C., Rappuoli, R., & Scarlato, V. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03227.x · Cited by 73
Cornish, A. S., & Page, W. J. (1998) · Microbiology · doi:10.1099/00221287-144-7-1747 · Cited by 69
Mycobacterium tuberculosis FurA Autoregulates Its Own Expression
Sala, C., Forti, F., Florio, E. D., Canneva, F., Milano, A., Riccardi, G., & Ghisotti, D. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.18.5357-5362.2003 · Cited by 69
“Under iron-replete conditions, the Fur protein, using Fe(2) as a corepressor, binds to a 19-bp operator sequence located upstream of the Fur-regulated genes (2, 10, 11, 13).”
BackgroundAnalysis of the complexity of gene regulation by fur in Vibrio cholerae
Litwin, C. M., & Calderwood, S. B. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.1.240-248.1994 · Cited by 69
“dinate regulation of genes by iron depends on the protein Fur (ferric iron uptake regulator), which binds to an operator site, or Fur box, in the promoters of iron-regulated genes and represses gene transcription in the presence of sufficient iron (1, 8, 11, 12, 20, 36).”
BackgroundSayyed, R. Z., Seifi, S., Patel, P. R., Shaikh, S. S., Jadhav, H. P., & Enshasy, H. A. E. (2019) · Environmental Sustainability · doi:10.1007/s42398-019-00070-4 · Cited by 68
Aminochelin, a Catecholamine Siderophore Produced by Azotobacter vinelandii
Page, W. J., & von Tigerstrom, M. (1988) · Microbiology · doi:10.1099/00221287-134-2-453 · Cited by 69
Ferric reductase activity in Azotobacter vinelandii and its inhibition by Zn2+
Huyer, M., & Page, W. J. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.7.4031-4037.1989 · Cited by 68
“Inasmuch as Fe2 , in a free, intracellular pool, has been proposed to be the major controlling factor for iron uptake (10, 39), lower levels of this ion resulting from the presence of Zn2+ could explain the observed increase in siderophore synthesis in A.”
BackgroundKinetics of toxA and regA mRNA accumulation in Pseudomonas aeruginosa
Frank, D. W., & Iglewski, B. H. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.10.4477-4483.1988 · Cited by 67
“The determination of which promoter is used can depend on a variety of environmental stimuli, including heat shock (10), ppGpp (18), UV light (31), cyclic AMP-CRP (1), nitrogen limitation (30), and iron limitation (7, 13).”
BackgroundDubrac, S., & Touati, D. (2002) · Microbiology · doi:10.1099/00221287-148-1-147 · Cited by 66
Characterization of the Shewanella oneidensis Fur gene: roles in iron and acid tolerance response
Yang, Y., Harris, D. P., Luo, F., Wu, L., Parsons, A. B., Palumbo, A. V., & Zhou, J. Z. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-s1-s11 · Cited by 66
Zn 2+ Increases Siderophore Production in Azotobacter vinelandii
Huyer, M., & Page, W. J. (1988) · Applied and Environmental Microbiology · doi:10.1128/aem.54.11.2625-2631.1988 · Cited by 63
“Zn2 ' is rather an anomalous ion since it only partially activates Fur and also acts to decrease the ability of Mn2 + to activate the Fur protein (9).”
Grossman, T. H., Tuckman, M., Ellestad, S., & Osburne, M. S. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.19.6203-6211.1993 · Cited by 65
“coli Fur box has been shown to bind Fur repressor, a negative regulator which controls iron genes in response to iron availability (3).”
BackgroundFarrell, D. H., Mikesell, P., Actis, L. A., & Crosa, J. H. (1990) · Gene · doi:10.1016/0378-1119(90)90112-5 · Cited by 65
Postle, K. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.5.2287-2293.1990 · Cited by 61
Regulation of expression of the Pasteurella haemolytica leukotoxin determinant
Strathdee, C. A., & Lo, R. Y. C. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.11.5955-5962.1989 · Cited by 65
“Several regulatory systems in which multiple or tandem promoters are controlled differently have been characterized, including those responsive to heat shock (8), ppGpp (17), cyclic AMP-receptor protein (1), and Fe2+ limitation (4, 11).”
BackgroundTindale, A. E., Mehrotra, M., Ottem, D., & Page, W. J. (2000) · Microbiology · doi:10.1099/00221287-146-7-1617 · Cited by 64
“A putative promoter, characteristic of a typical E. coli σ(! promoter (Lewin, 1994) and a putative iron-box, having 14 out of 19 bp identical to the E. coli iron-box consensus sequence (de Lorenzo et al., 1987), was identified overlapping the ®35 region of the csbC promoter (Fig.”
BackgroundInfluential
Metadata
- 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
- 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
- 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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