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The ZnuABC high‐affinity zinc uptake system and its regulator Zur in Escherichia coli
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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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“ZnuABC is a high-affinity ABC-type zinc transporter best characterized in E. coli, consisting of a periplasmic binding protein (ZnuA), membrane permease (ZnuB), and ATPase (ZnuC) [196].”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [196]
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“The ZnuABC system is regulated by Zur, a metallo-regulatory protein of the Fur family, such that zinc import is repressed in zinc-replete conditions [196].”
From Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity (2012) · cites this paper as [196]
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“…in P. putida 7 © 2003 Society for Applied Microbiology and Blackwell Publishing Ltd, Environmental Microbiology highly homologous to E. coli znuACB. znuACB1Ppu is organized differently from E. coli, in which the regulatory protein zur is located elsewhere in the genome (Patzer and Hantke, 1998).”
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“The ZnuABC system is regulated by Zur, a metallo-regulatory protein of the Fur family, such that zinc import is repressed in zinc-replete conditions [196].”
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“In conclusion, our findings concerning virulence of the Salmonella serovar Typhimurium znuC mutant indicate that the znuABC system must be the principal one by which zinc uptake takes place in this bacterial species during mouse infection and give support to previous suggestions about the protective role that zinc-che…”
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“znuABC encodes a zinc ABC transporter which imports zinc into E. coli ( Patzer & Hantke, 1998 ).”
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“…Fur-family regulator 1853 © 2006 The Authors Journal compilation © 2006 Blackwell Publishing Ltd, Molecular Microbiology, 59, 1848–1858 This parallels the effect of Fur and Zur in negatively regulating iron and zinc uptake, respectively, in E. coli (Hantke, 1981; Patzer and Hantke, 1998).”
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“E. coli Zur is a recently discovered Fur ortholog (27% sequence identity) that regulates the expression of a divergently transcribed operon that encodes the high affinity zinc uptake system, znuBC and znuA, in a highly Zn(II)-specific fashion (Patzer & Hantke 1998, 2000).”
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“The genes of this operon encode the periplasmic substrate-binding protein, the ATPase and the integral inner membrane component, respectively, of an ABC transporter required for the transport of zinc from the periplasm into the cytoplasm [19].”
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BackgroundMycobacterial FurA is a negative regulator of catalase-peroxidase gene katG
Zahrt, T. C., Song, J., Siple, J., & Deretic, V. P. (2001) · Molecular Microbiology · doi:10.1111/j.1365-2958.2001.02321.x · Cited by 136
Zhang, Y., & Gladyshev, V. N. (2009) · Chemical Reviews · doi:10.1021/cr800557s · Cited by 143
Iwig, J. S., Rowe, J. L., & Chivers, P. T. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05369.x · Cited by 134
“Zinc regulation is accomplished by a pair of proteins, Zur (Patzer and Hantke, 1998) and ZntR (Brocklehurst et al.”
BackgroundInfluentialPetrarca, P., Ammendola, S., Pasquali, P., & Battistoni, A. (2010) · Journal of Bacteriology · doi:10.1128/jb.01310-09 · Cited by 129
“Investigations initially carried out in Escherichia coli and then confirmed in other microorganisms have established that zinc homeostasis is finely controlled by the coordinated activity of import and export systems regulated by Zur and ZntR, two metalloproteins able to regulate gene transcription depending on their…”
BackgroundTransition metal ions at the crossroads of mucosal immunity and microbial pathogenesis
Diaz-Ochoa, V. E., Jellbauer, S., Klaus, S., & Raffatellu, M. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00002 · Cited by 129
“High-affinity ABC-type zinc transporters include ZnuABC of Gram-negative bacteria (Patzer and Hantke, 1998; Hantke, 2005), and AdcBCA of the Grampositive streptococci (Dintilhac et al.”
BackgroundSabri, M., Houle, S., & Dozois, C. M. (2009) · Infection and Immunity · doi:10.1128/iai.01082-08 · Cited by 118
“coli K-12 znu genes have been shown to be induced under iron repletion and repressed under iron depletion (44).”
BackgroundMethodBacterial metal-sensing proteins exemplified by ArsR–SmtB family repressors
Osman, D., & Cavet, J. S. (2010) · Natural Product Reports · doi:10.1039/b906682a · Cited by 129
Functional Analysis of theBacillus subtilisZur Regulon
Gaballa, A., Wang, T., Ye, R. W., & Helmann, J. D. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.23.6508-6514.2002 · Cited by 123
“coli (25), and homologs have been identified in Listeria monocytogenes (8) and Staphylococcus aureus (20).”
BackgroundZinc Competition among the Intestinal Microbiota
Gielda, L. M., & DiRita, V. J. (2012) · mBio · doi:10.1128/mbio.00171-12 · Cited by 121
“coli, Salmonella enterica, Proteus mirabilis, Haemophilus influenzae, and Brucella abortus (13-15, 21-23).”
BackgroundMicrobial Zinc Solubilization and Their Role on Plants
Saravanan, V. S., Kumar, M., & Sa, T. M. (2011) · Springer eBooks · doi:10.1007/978-3-642-21061-7_3 · Cited by 119
“It was demonstrated in Escherichia coli ( Patzer and Hantke 1998 ) and also in Streptococcus pneumoniae.”
BackgroundShin, J., Oh, S., Kim, S., & Roe, J. (2007) · Journal of Bacteriology · doi:10.1128/jb.01851-06 · Cited by 118
“Examples of the metalspecific Fur family regulators are Zur for zinc (39), Mur for manganese (13), and Nur for nickel (2).”
BackgroundBinet, M. R. B., & Poole, R. K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01509-x · Cited by 118
Davis, L. M., Kakuda, T., & DiRita, V. J. (2008) · Journal of Bacteriology · doi:10.1128/jb.01394-08 · Cited by 118
“coli, Salmonella enterica, Brucella abortus, Neisseria gonorrhoeae, Pasteurella multocida, and Haemophilus species (20, 25, 30, 31).”
BackgroundInfluentialStructural and Mechanistic Basis of Zinc Regulation Across the E. coli Zur Regulon
Gilston, B. A., Wang, S., Marcus, M. D., Canalizo-Hernández, M. A., Swindell, E. P., Xue, Y., Mondragón, A., & O’Halloran, T. V. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001987 · Cited by 118
“Intriguingly, this small protein (19 kDa) protects an unexpectedly large region (,30 bp) of the znuABC (PznuABC), the L31p (PL31p), and zinT (PzinT) operators under Zn -saturating conditions [14].”
BackgroundZinc fingers can act as Zn2+ sensors to regulate transcriptional activation domain function
Bird, A. J., McCall, K., Kramer, M., Blankman, E., Winge, D. R., & Eide, D. J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg484 · Cited by 117
Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli
Yatsunyk, L. A., Easton, J. A., Kim, L. R., Sugarbaker, S. A., Bennett, B., Breece, R. M., Vorontsov, I. I., Tierney, D. L., Crowder, M. W., & Rosenzweig, A. C. (2007) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-007-0320-0 · Cited by 116
Bacterial zinc uptake regulator proteins and their regulons
Mikhaylina, A., Ksibe, A. Z., Scanlan, D. J., & Blindauer, C. A. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170228 · Cited by 116
Multiple Regulatory Mechanisms Maintain Zinc Homeostasis in Saccharomyces cerevisiae
Eide, D. J. (2003) · Journal of Nutrition · doi:10.1093/jn/133.5.1532s · Cited by 115
Binet, M. R. B., Ma, R., McLeod, C. W., & Poole, R. K. (2003) · Analytical Biochemistry · doi:10.1016/s0003-2697(03)00190-8 · Cited by 112
Kobayashi, M., Ishizuka, T., Katayama, M., Kanehisa, M. I., Bhattacharyya‐Pakrasi, M., Pakrasi, H. B., & Ikeuchi, M. (2004) · Plant and Cell Physiology · doi:10.1093/pcp/pch034 · Cited by 114
“tein in E. coli ( Patzer and Hantke 1998 ) and Bacillus subtilis (Gaballa and Helmann 1998).”
BackgroundBanerjee, S., Wei, B., Bhattacharyya-Pakrasi, M., Pakrasi, H. B., & Smith, T. J. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.008 · Cited by 113
ZntR-mediated transcription of zntA responds to nanomolar intracellular free zinc
Wang, D., Hosteen, O., & Fierke, C. A. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.02.008 · Cited by 114
Beard, S. J., Hashim, R., Wu, G., Binet, M. R. B., Hughes, M., & Poole, R. K. (2000) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2000.tb09019.x · Cited by 111
“coli, in contrast to the ZnuABC high-a¤nity uptake system that has been described recently [10].”
BackgroundResultIssues underlying use of biosensors to measure metal bioavailability
Rensing, C., & Maier, R. M. (2003) · Ecotoxicology and Environmental Safety · doi:10.1016/s0147-6513(03)00057-5 · Cited by 117
A systems view of haloarchaeal strategies to withstand stress from transition metalsPreprint
Kaur, A., Pan, M., Meislin, M., Facciotti, M. T., El-Gewely, R., & Baliga, N. S. (2006) · Genome Research · doi:10.1101/gr.5189606 · Cited by 114
“If so, then DIP might also be chelating some other divalent ion(s), such as Zn(II) (Patzer and Hantke 1998), which are in limited supply in the growth medium for Halobacterium NRC-1.”
BackgroundCompetition for zinc binding in the host-pathogen interaction
Cerasi, M., Ammendola, S., & Battistoni, A. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00108 · Cited by 114
“…is composed of three proteins: the ZnuB channel, the ZnuC ATPase component which provides the energy necessary for ion transport through the inner membrane, and ZnuA, a soluble protein which captures Zn(II) in the periplasm with high efficiency and delivers it to ZnuB (Patzer and Hantke, 1998).”
BackgroundFahsi, N., Mahdi, I., Mesfioui, A., Biskri, L., & Allaoui, A. (2021) · Agriculture · doi:10.3390/agriculture11040316 · Cited by 108
“coli [71], ZnuC, encoding for a predictive Zn ABC transporter periplasmic”
BackgroundZinc: Multidimensional Effects on Living Organisms
Cuajungco, M. P., Ramirez, M. S., & Tolmasky, M. E. (2021) · Biomedicines · doi:10.3390/biomedicines9020208 · Cited by 107
“A major import mechanism is ZnuABC, an ATP-binding cassette (ABC) transporter [95,96].”
BackgroundA Gene Cluster Involved in Metal Homeostasis in the Cyanobacterium Synechocystis sp. Strain PCC 6803
García‐Domínguez, M., López‐Maury, L., Florencio, F. J., & Reyes, J. C. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.6.1507-1514.2000 · Cited by 102
Gabbianelli, R., Scotti, R., Ammendola, S., Petrarca, P., Nicolini, L., & Battistoni, A. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-36 · Cited by 107
“In contrast, when bacteria grow in environments characterized by very low zinc availability, zinc import is ensured by the high affinity zinc transporter ZnuABC [4,11], whose synthesis is tightly controlled by the binding of this metal to the promoter of zur gene [12].”
BackgroundResultMortensen, B. L., & Skaar, E. P. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00095 · Cited by 99
“…in numerous bacterial species such as Campylobacter jejuni, Salmonella, Neisseria meningitidis, E. coli, and Y. pestis and in some cases demonstrated to be required for virulence (Patzer and Hantke, 1998; Campoy et al., 2002; Ammendola et al., 2007; Davis et al., 2009; Stork et al., 2010).”
Background
Metadata
- 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
- 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
- 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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