Cited by 490Bacterial Genetics and BiotechnologyTrace Elements in HealthEscherichia coli research studies

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The ZnuABC high‐affinity zinc uptake system and its regulator Zur in Escherichia coli

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Patzer, Silke I., Hantke, Klaus·1998·Molecular Microbiology

DOI 10.1046/j.1365-2958.1998.00883.x

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Abstract

In Escherichia coli, lacZ operon fusions were isolated that were derepressed under iron repletion and repressed under iron depletion. Two fusions were localized in genes that formed an operon whose gene products had characteristics of a binding protein‐dependent transport system. The growth defect of these mutants on TY medium containing 5 mM EGTA was compensated for by the addition of Zn 2+. In the presence of 0.5 mM EGTA, only the parental strain was able to take up 65 Zn 2+. This high‐affinity transport was energized by ATP. The genes were named znuACB (for zinc uptake; former name yebLMI ) and localized at 42 min on the genetic map of E. coli. At high Zn 2+ concentrations, the znu mutants took up more 65 Zn 2+ than the parental strain. The high‐affinity 65 Zn 2+ uptake was repressed by growth in the presence of 10 μM Zn 2+. A znuA–lacZ operon fusion was repressed by 5 μM Zn 2+ and showed a more than 20‐fold increase in β‐galactosidase activity when Zn 2+ was bound to 1.5 μM TPEN [tetrakis‐(2‐pyridylmethyl) ethylenediamine]. To identify the Zn 2+‐dependent regulator, constitutive mutants were isolated and tested for complementation by a gene bank of E. coli. A complementing gene, yjbK of the E. coli genome, was identified and named zur (for zinc uptake regulation). The Zur protein showed 27% sequence identity with the iron regulator Fur. High‐affinity 65 Zn 2+ transport of the constitutive zur mutant was 10‐fold higher than that of the uninduced parental strain. An in vivo titration assay suggested that Zur binds to the bidirectional promoter region of znuA and znuCB.

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
Experiments in molecular genetics
Miller, J. H. (1972) · Medical Entomology and Zoology · Cited by 27,157
Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetii
Voth, D. E., & Heinzen, R. A. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00901.x · Cited by 11,764
The complete genome sequence of Escherichia coli K-12.
Blattner, F., Plunkett, G., Bloch, C., Perna, N., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C., Mayhew, G., et al. (1997) · Science · doi:10.1126/science.277.5331.1453 · Cited by 7,996
Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
Chang, A. C. Y., & Cohen, S. N. (1978) · Journal of Bacteriology · doi:10.1128/jb.134.3.1141-1156.1978 · Cited by 4,261
A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes.
Tabor, S., & Richardson, C. C. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.4.1074 · Cited by 3,165
Experiments With Gene Fusions
Silhavy, T. J., Berman, M. L., & Enquist, L. W. (1984) · Medical Entomology and Zoology · Cited by 2,406
Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria
Postma, P. W., Lengeler, J. W., & Jacobson, G. R. (1993) · Microbiological Reviews · doi:10.1128/mr.57.3.543-594.1993 · Cited by 1,802
Improved single and multicopy lac-based cloning vectors for protein and operon fusions
Simons, R. W., Houman, F., & Kleckner, N. E. (1987) · Gene · doi:10.1016/0378-1119(87)90095-3 · Cited by 1,531

Show all 53 references

Research works printed but not linked: 2

Sambrook J. Fritsch E.F. Maniatis T.(1989)Molecular Cloning: a Laboratory Manual 2nd edn. Cold Spring Harbor NY: Cold Spring Harbor Laboratory Press.
Tabor S.(1996) Protein expression. InCurrent Protocols in Molecular Biology. Ausubel F.M. Brent R. Kingston R.E. Moore D.D. Seidman J.G. Smith J.A. and Struhl K. (eds.). New York: John Wiley & Sons.

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Background
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BackgroundInfluential
The Zur of Xanthomonas campestris functions as a repressor and an activator of putative zinc homeostasis genes via recognizing two distinct sequences within its target promoters
Huang, D., Tang, D., Liao, Q., Li, H.-C., Chen, Q., He, Y.-Q., Feng, J., Jiang, B., Lu, G., Chen, B., et al. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn328 · Cited by 63
“Zur was first described as a negative transcriptional regulator of genes encoding Zn-uptake systems in Escherichia coli (5) and Bacillus subtilis (6).”
Background
A Fur-like protein PerR regulates two oxidative stress response related operons dpr and metQIN in Streptococcus suis
Zhāng, T., Ding, Y., Li, T., Wan, Y., Li, W., Chen, H., & Zhou, R. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-85 · Cited by 61
“They are the sensors of iron (Fur and Irr) [8] [9], zinc (Zur) [10], manganese [11] and nickel (Nur) [12], and the peroxide regulon repressor (PerR) [13].”
Background
An overview of the biological metal uptake pathways in P seudomonas aeruginosa
Schalk, I. J., & Cunrath, O. (2016) · Environmental Microbiology · doi:10.1111/1462-2920.13525 · Cited by 65
Zinc Uptake Contributes to Motility and Provides a Competitive Advantage to Proteus mirabilis during Experimental Urinary Tract Infection
Nielubowicz, G. R., Smith, S. N., & Mobley, H. L. T. (2010) · Infection and Immunity · doi:10.1128/iai.01220-09 · Cited by 61
“coli, this process is achieved via the ZnuACB system (51).”
Background
Iron Transport in Escherichia Coli: All has not been said and Done
Grass, G. (2006) · BioMetals · doi:10.1007/s10534-005-4341-2 · Cited by 60
“…cells expressing zupT from a plasmid exhibited increased uptake of Zn(II) (Grass et al. 2002) and deletion mutants of zupT and znuABC, the high-affinity Zn(II) ABCuptake system of E. coli (Patzer & Hantke 1998), responded stronger to zinc-deprivation than a znuABC single mutant (Grass et al. 2002).”
Background
Impact of Manganese, Copper and Zinc Ions on the Transcriptome of the Nosocomial Pathogen Enterococcus faecalis V583
Abrantes, M. C., Lopes, M. D. F., & Kok, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026519 · Cited by 60
Trace Metal Acquisition by Marine Heterotrophic Bacterioplankton with Contrasting Trophic Strategies
Hogle, S., Thrash, J. C., Dupont, C. L., & Barbeau, K. A. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.03128-15 · Cited by 60
“Some TroAfamily ABCT substrate binding proteins (23) participate in the uptake of Mn(2) (24), Zn(2) (25), and vitamin B12 (26).”
Background
Zinc Chelation by a Small-Molecule Adjuvant Potentiates Meropenem Activity in Vivo against NDM-1-Producing Klebsiella pneumoniae
Falconer, S. B., Reid‐Yu, S. A., King, A. M., Gehrke, S. S., Wang, W., Britten, J. F., Coombes, B. K., Wright, G. D., & Brown, E. D. (2015) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.5b00033 · Cited by 59
The Transcriptional Regulator Np20 Is the Zinc Uptake Regulator in Pseudomonas aeruginosa
Ellison, M. L., Farrow, J. M., Parrish, W., Danell, A. S., & Pesci, E. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075389 · Cited by 58
Pseudomonas aeruginosa zinc homeostasis: Key issues for an opportunistic pathogen
Gonzalez, M. R., Ducret, V., Leoni, S., & Perron, K. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.01.018 · Cited by 57
Fur Is Involved in Manganese-Dependent Regulation of mntA ( sitA ) Expression in Sinorhizobium meliloti
Platero, R., Peixoto, L., O’Brian, M. R., & Fabiano, E. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.7.4349-4355.2004 · Cited by 59
The Fur Homologue inBorrelia burgdorferi
Katona, L. I., Tokarz, R., Kuhlow, C. J., Benach, J., & Benach, J. L. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.19.6443-6456.2004 · Cited by 58
“Zur is a Fur homologue that regulates uptake of zinc by the Znu ABC transporter system (43, 44).”
Background
Fine control of metal concentrations is necessary for cells to discern zinc from cobalt
Osman, D., Foster, A. W., Chen, J., Svedaite, K., Steed, J. W., Lurie-Luke, E., Huggins, T. G., & Robinson, N. J. (2017) · Nature Communications · doi:10.1038/s41467-017-02085-z · Cited by 58
Fur-like proteins: Beyond the ferric uptake regulator (Fur) paralog
Sevilla, E., Bes, M. T., Peleato, M. L., & Fillat, M. F. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108770 · Cited by 59
The Zinc-Responsive Regulon of Neisseria meningitidis Comprises 17 Genes under Control of a Zur Element
Pawlik, M.-C., Hubert, K., Joseph, B., Claus, H., Schoen, C. U., & Vogel, U. F. (2012) · Journal of Bacteriology · doi:10.1128/jb.01091-12 · Cited by 57
“(45), Bacillus subtilis (13), Listeria monocytogenes (7), and Staph-”
Background
Ligand-Controlled Proteolysis of the Escherichia coli Transcriptional Regulator ZntR
Pruteanu, M., Neher, S. B., & Baker, T. A. (2007) · Journal of Bacteriology · doi:10.1128/jb.01531-06 · Cited by 58
“coli is ZnuABC, an ABC-type transporter (33, 34), and the primary zinc export system is the P-type ATPase ZntA (37).”
Background
Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking
Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 64
New insights into the role of Fur proteins: FurB (All2473) from Anabaena protects DNA and increases cell survival under oxidative stress
López-Gomollón, S., Sevilla, E., Bes, M. T., Peleato, M. L., & Fillat, M. F. (2008) · Biochemical Journal · doi:10.1042/bj20081066 · Cited by 56
Transcriptional Response ofEscherichia colito TPEN
Sigdel, T. K., Easton, J. A., & Crowder, M. W. (2006) · Journal of Bacteriology · doi:10.1128/jb.00680-06 · Cited by 56
Expression of the PitA phosphate/metal transporter ofEscherichia coliis responsive to zinc and inorganic phosphate levels
Jackson, R., Binet, M. R. B., Lee, L. J., Ma, R., Graham, A. I., McLeod, C. W., & Poole, R. K. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2008.01386.x · Cited by 59
“The major inducible high-affinity Zn(II) uptake system is the ABC transporter, ZnuABC (Patzer & Hantke, 1998), but a further broad substrate, low affinity, constitutive zinc uptake system exists, ZupT (Grass et al., 2005), and Zn(II) also enters via the Pit system (Beard et al., 2000).”
Background
Manganese and Zinc Regulate Virulence Determinants in Borrelia burgdorferi
Troxell, B., Ye, M., Yang, Y., Carrasco, S. E., Lou, Y., & Yang, X. (2013) · Infection and Immunity · doi:10.1128/iai.00507-13 · Cited by 55
YeiR: a metal-binding GTPase from Escherichia coli involved in metal homeostasis
Blaby-Haas, C. E., Flood, J. A., Crécy-Lagard, V. D., & Zamble, D. B. (2012) · Metallomics · doi:10.1039/c2mt20012k · Cited by 54
The effect of zinc limitation on the transcriptome of P seudomonas protegens Pf ‐5
Lim, C. K., Hassan, K. A., Penesyan, A., Loper, J. E., & Paulsen, I. T. (2012) · Environmental Microbiology · doi:10.1111/j.1462-2920.2012.02849.x · Cited by 55
“In many bacterial species, ZnuABC is the major uptake system for zinc (Patzer and Hantke, 1998; Ammendola et al., 2007; Desrosiers et al., 2010).”
Background
MucR Is Required for Transcriptional Activation of Conserved Ion Transporters to Support Nitrogen Fixation of Sinorhizobium fredii in Soybean Nodules
Jiao, J., Wu, L., Zhang, B., Hu, Y., Li, Y., Zhang, X. X., Guo, H. J., Liu, L. X., Chen, W. X., Zhang, Z., et al. (2016) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-01-16-0019-r · Cited by 54
“…membrane (Moreau et al. 2002). znuA, znuB, and znuC encode the conserved bacterial zinc transport system importing zinc under low zinc conditions (Patzer and Hantke 1998; VahlingArmstrong et al. 2012), and they were strongly induced in CCBAU45436 bacteroids compared with free-living cells (log2…”
Background
Coordinated regulation of core and accessory genes in the multipartite genome of Sinorhizobium fredii
Jiao, J., Ni, M., Zhang, B., Zhang, Z., Young, J. P. W., Chan, T., Chen, W. X., Lam, H., & Tian, C. F. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007428 · Cited by 54
“The zinc transporter encoded by znu can import zinc under low-zinc conditions [43,44].”
Background
Genome analysis and characterization of zinc efflux systems of a highly zinc-resistant bacterium, Comamonas testosteroni S44
Xiong, J., Li, D., Li, H., He, M., Miller, S. J., Yu, L., Rensing, C., & Wang, G. (2011) · Research in Microbiology · doi:10.1016/j.resmic.2011.06.002 · Cited by 53
“In Escherichia coli, the znuABC operon encoding the high affinity Zn2þ uptake system is negatively controlled by Zur (Patzer and Hantke, 1998), acting as a repressor to prevent entry of RNA polymerase into promoter regulating znuABC (Shin et al., 2007).”
Background
Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other Alpha-proteobacteria
Small, S. K., Puri, S., & O’Brian, M. R. (2008) · BioMetals · doi:10.1007/s10534-008-9192-1 · Cited by 53
“Irr protein belongs to the Fur family of metalloregulators that includes Fur, PerR, Zur, Nur, and Mur (Bsat et al. 1998; Gaballa and Helmann 1998; Hamza et al. 1998; Patzer and Hantke 1998; Chao et al. 2004; Diaz-Mireles et al. 2004; Platero et al. 2004; Ahn et al. 2006).”
Influential
Three fur homologues from Anabaena sp. PCC7120: exploring reciprocal protein-promoter recognition
Hernández, J. L., LÃ³pez-GomollÃ³n, S., Bes, M. T., Fillat, M. F., & Peleato, M. L. (2004) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2004.05.050 · Cited by 58
Insights into the Antibacterial Mechanism of Action of Chelating Agents by Selective Deprivation of Iron, Manganese, and Zinc
Paterson, J. R., Beecroft, M. S., Mulla, R. S., Osman, D., Reeder, N. L., Caserta, J. A., Young, T. R., Pettigrew, C. A., Davies, G. E., Williams, J. A. G., et al. (2021) · Applied and Environmental Microbiology · doi:10.1128/aem.01641-21 · Cited by 53
“Another ABC family transporter, ZnuABC, transports Zn(II) across the inner membrane (72, 84).”
Background
Characterisation of a new operon encoding a Zur-like protein and an associated ABC zinc permease in Listeria monocytogenes
Dalet, K., Gouin, E., Cenatiempo, Y., Cossart, P., & Héchard, Y. (1999) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1999.tb13556.x · Cited by 52
A bacterial protease depletes c-MYC and increases survival in mouse models of bladder and colon cancer
Butler, D. S. C., Cafaro, C., Putze, J., Wan, M. L. Y., Tran, T. H., Ambite, I., Ahmadi, S., Kjellström, S., Welinder, C., Chao, S. M., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-020-00805-3 · Cited by 51
Three fur homologues from Anabaena sp. PCC7120: exploring reciprocal protein-promoter recognition
HernÃ¡ndez, J. A., López-Gomollón, S., Bes, M. T., Fillat, M. F., & Peleato, M. L. (2004) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2004.tb09658.x · Cited by 51
Manganese uptake and streptococcal virulence
Eijkelkamp, B. A., McDevitt, C. A., & Kitten, T. O. (2015) · BioMetals · doi:10.1007/s10534-015-9826-z · Cited by 50
“…1999, 2002); YfeA_Ype, GI:1245464 (Bearden and Perry 1999; Bearden et al. 1998); ZnuA_Cje, GI:384442496 (Davis et al. 2009); ZnuA_Eco, GI:298380994 (Patzer and Hantke 1998); ZnuA_Hin, GI:16272089 (Lu et al. 1997); ZnuA_Sen, GI:161353595 (Ammendola et al. 2007; Ilari et al. 2011); ZnuA_Syn,…”
Regulation and Activity of a Zinc Uptake Regulator, Zur, in Corynebacterium diphtheriae
Smith, K. F., Bibb, L. A., Schmitt, M. P., & Oram, D. M. (2008) · Journal of Bacteriology · doi:10.1128/jb.01392-08 · Cited by 49
“Zinc uptake is controlled in a zinc-dependent manner by Zur in bacteria such as E. coli, Bacillus subtilis, and M. tuberculosis (14, 23, 34 ).”
Background
Zinc dependence of zinT (yodA) mutants and binding of zinc, cadmium and mercury by ZinT
Kershaw, C. J., Brown, N. L., & Hobman, J. L. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.094 · Cited by 49
Identification of a Functional fur Gene in Bradyrhizobium japonicum
Hamza, I., Hassett, R. F., & O’Brian, M. R. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.18.5843-5846.1999 · Cited by 48
“coli and Bacillus subtilis; these proteins are involved in the maintenance of zinc homeostasis (Zur) (7, 12), or in a manganese-dependent response to oxidative stress (PerR) (3).”
Background
Diadenosine tetraphosphate (Ap4A) – an E. coli alarmone or a damage metabolite?
Despotović, D., Brandis, A. S., Savidor, A., Levin, Y., Fumagalli, L., & Tawfik, D. S. (2017) · FEBS Journal · doi:10.1111/febs.14113 · Cited by 48
Zur: Zinc-Sensing Transcriptional Regulator in a Diverse Set of Bacterial Species
Kandari, D., Joshi, H., & Bhatnagar, R. (2021) · Pathogens · doi:10.3390/pathogens10030344 · Cited by 46
“aeruginosa led to the identification of a zur-like gene, np20, which when disrupted resulted in the reduction of virulence in the mouse models [71].”
BackgroundInfluential
Unravelling the antibiotic and heavy metal resistome of a chronically polluted soil
Salam, L. B. (2020) · 3 Biotech · doi:10.1007/s13205-020-02219-z · Cited by 48
Copper-resistant halophilic bacterium isolated from the polluted Maruit Lake, Egypt
Osman, O. A., Tanguichi, H., Ikeda, K., Park, P., Tanabe-Hosoi, S., & Nagata, S. (2009) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2009.04574.x · Cited by 48
“Furthermore, zinc transport protein ZnuC was identified in pMA22, resembling the high affinity binding protein dependent transport system for zinc (Znu ABC) reported in E. coli (Patzer and Hantke 1998).”
Background
Endopeptidase Regulation as a Novel Function of the Zur-Dependent Zinc Starvation Response
Murphy, S. G., Alvarez, L., Adams, M. C., Liu, S., Chappie, J. S., Cava, F., & Dörr, T. (2019) · mBio · doi:10.1128/mbio.02620-18 · Cited by 46
“Zur is a fur-family transcriptional regulator and 115 the central repressor in the zinc starvation response (25).”
Background
Elevated zinc induces siderophore biosynthesis genes and a zntA-like gene in Pseudomonas fluorescens
Rossbach, S., Wilson, T. L., Kukuk, M. L., & Carty, H. A. (2000) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2000.tb09320.x · Cited by 47
The Mycobacterium tuberculosis Rv2358–furB operon is induced by zinc
Milano, A., Branzoni, M., Canneva, F., Profumo, A., & Riccardi, G. (2003) · Research in Microbiology · doi:10.1016/j.resmic.2003.11.009 · Cited by 47
Zinc Uptake Regulator (zur) Gene Involved in Zinc Homeostasis and Virulence of Xanthomonas oryzae pv. oryzae in Rice
Yang, W., Liú, Y., Chen, L., Gao, T., Hu, B., Zhang, D., & Liu, F. (2007) · Current Microbiology · doi:10.1007/s00284-006-0485-8 · Cited by 45
“coli, the zinc uptake system ZnuABC is negatively regulated by Zur [26].”
Background
A Novel DNA-binding Site for the Ferric Uptake Regulator (Fur) Protein from Bradyrhizobium japonicum
Friedman, Y. E., & O’Brian, M. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306710200 · Cited by 45
Fate of antibiotic resistance genes and EPS defence mechanisms during simultaneous denitrification and methanogenesis, coupled with the biodegradation of multiple antibiotics under zinc stress
Zheng, J., Wang, S., Gong, Q., Zhou, A., Liang, B., Zhao, B., Li, H., Zhang, X., Yang, Y., & Yue, X. (2024) · Water Research · doi:10.1016/j.watres.2024.121996 · Cited by 44
Role of the N-terminus in Determining Metal-Specific Responses in the E. coli Ni- and Co-Responsive Metalloregulator, RcnR
Higgins, K. A., Chivers, P. T., & Maroney, M. J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja300834b · Cited by 44

Authors: Patzer, S. I., & Hantke, K.
Affiliations: University of Tübingen (DE)
Corresponding author: Hantke, Klaus
ORCID: Hantke, Klaus
Venue: Molecular Microbiology
Publisher: Wiley
Published: 1998-06
Volume: 28
Issue: 6
Pages: 1199-1210
ISSN: 0950-382X (ISSN-L)
1365-2958
DOI: 10.1046/j.1365-2958.1998.00883.x
OpenAlex: W2139802399
Cited by: 490
References: 53
Citations by year: 2026: 19 · 2025: 12 · 2024: 19 · 2023: 9 · 2022: 18 · 2021: 25 · 2020: 12 · 2019: 22 · 2018: 22 · 2017: 23 · 2016: 17 · 2015: 18 · 2014: 18 · 2013: 20 · 2012: 22
FWCI: 7.61
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 1631 d)
Locations: Molecular Microbiology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
Keywords: Zur, zinc uptake, binding protein-dependent transport, iron regulation, transcriptional regulation, Escherichia coli
MeSH terms: Amino Acid Sequence, Autoradiography, Bacterial Proteins, beta-Galactosidase, Chromosome Mapping, DNA-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Genes, Regulator, Genetic Complementation Test, Lac Operon, Molecular Sequence Data, Mutation, Operon, Time Factors, Zinc, Gene Expression Regulation, Bacterial, Ion Transport, ATP-Binding Cassette Transporters, Artificial Gene Fusion, Escherichia coli Proteins

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The ZnuABC high‐affinity zinc uptake system and its regulator Zur in Escherichia coli

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