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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Lactococcus lactis ZitR Is a Zinc-Responsive Repressor Active in the Presence of Low, Nontoxic Zinc Concentrations In Vivo
Llull, D., Son, O., Blanié, S., Briffotaux, J., Morello, E., Rogniaux, H., Danot, O., & Poquet, I. (2011) · Journal of Bacteriology · doi:10.1128/jb.01109-10 · Cited by 29
“Lactococcus lactis ZitR Is a Zinc-Responsive Repressor Active in the Presence of Low, Nontoxic Zinc Concentrations In Vivo † Daniel Llull,1§‡ Olivier Son,1§ Sandrine Blanié,2 Julien Briffotaux,1¶ Eric Morello,1 Hélène Rogniaux,3 Olivier Danot,4 and Isabelle Poquet1* INRA, UMR1319 Micalis (Microbiologie de l’Aliment…”
BackgroundMethodInfluential
Agrobacterium tumefaciens Zur Regulates the High-Affinity Zinc Uptake System TroCBA and the Putative Metal Chaperone YciC, along with ZinT and ZnuABC, for Survival under Zinc-Limiting Conditions
Chaoprasid, P., Dokpikul, T., Johnrod, J., Sirirakphaisarn, S., Nookabkaew, S., Sukchawalit, R., & Mongkolsuk, S. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.00299-16 · Cited by 29
Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin)
Cunden, L. S., Brophy, M. B., Rodriguez, G. E., Flaxman, H. A., & Nolan, E. M. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00781 · Cited by 30
“the parent strain.(46) We previously used the ΔznuA mutant as tool for probing Zn(II) sequestration by human S100A12,(41) and reasoned that experiments with this mutant”
Method
Effects of zinc on the production of alcohol byClostridium carboxidivoransP7 using model syngas
Li, D., Meng, C., Wu, G., Xie, B., Han, Y., Guo, Y., Song, C., Gao, Z., & Huang, Z. (2017) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-017-1992-2 · Cited by 29
“Therefore, in bacteria, zinc ions must be tightly regulated [27].”
Background
Comparative genomics and metagenomics of the metallomes
Zhang, Y., Ying, H., & Xu, Y. (2019) · Metallomics · doi:10.1039/c9mt00023b · Cited by 29
Novel MntR-Independent Mechanism of Manganese Homeostasis in Escherichia coli by the Ribosome-Associated Protein HflX
Kaur, G., Sengupta, S., Kumar, V., Kumari, A., Ghosh, A., Parrack, P., & Dutta, D. (2014) · Journal of Bacteriology · doi:10.1128/jb.01717-14 · Cited by 27
“Mn-mediated activation of Fur, Fe-mediated activation of MntR, or Mnmediated inactivation of Zur, have also been proposed (10, 30, 34, 35, 36).”
BackgroundInfluential
Physicochemical Evidence that Treponema pallidum TroA Is a Zinc-Containing Metalloprotein That Lacks Porin-Like Structure
Deka, R. K., Lee, Y.-H., Hagman, K. E., Shevchenko, D., Lingwood, C. A., Hasemann, C. A., Norgard, M. V., & Radolf, J. D. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.14.4420-4423.1999 · Cited by 29
“As noted earlier, TroA shares sequence homology with known periplasmic metalbinding proteins (1, 2, 10, 14, 15, 17, 19).”
Background
Metal Ion Uptake and Oxidative Stress
Herbig, A. F., & Helmann, J. D. (2014) · ASM Press eBooks · doi:10.1128/9781555817992.ch29 · Cited by 29
Structures, Mechanisms, and Physiological Functions of Zinc Transporters in Different Biological Kingdoms
Bui, H. B., & Inaba, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25053045 · Cited by 28
“It comprises three protein subunits: A periplasmic Zn 2+ -binding protein (ZnuA), an integrated membrane protein that transports Zn 2+ across the cytoplasmic membrane (ZnuB), and an ATPase protein in charge of coupling Zn 2+ transport to ATP hydrolysis (ZnuC) [124,125].”
Background
Revealing the role of Plant Growth Promoting Rhizobacteria in suppressive soils against Fusarium oxysporum f.sp. cubense based on metagenomic analysis
Nisrina, L., Effendi, Y., & Pancoro, A. (2021) · Heliyon · doi:10.1016/j.heliyon.2021.e07636 · Cited by 28
“Its system is encoded by ZnuABC that has a high affinity to uptake metals (Patzer and Hantke, 1998).”
Background
Transition Metal Homeostasis
Nies, D. H., & Grass, G. (2009) · EcoSal Plus · doi:10.1128/ecosalplus.5.4.4.3 · Cited by 31
“Regulatory circuits involving zinc The expression of the ZnuABC uptake system is under the control of the Zur protein (29), a paralog of the main iron homeostasis regulator Fur.”
Background
Carbon Availability Modifies Temperature Responses of Heterotrophic Microbial Respiration, Carbon Uptake Affinity, and Stable Carbon Isotope Discrimination
Min, K., Lehmeier, C., Ballantyne, F., & Billings, S. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.02083 · Cited by 28
“…interest at multiple scales and levels of organization, from microbes to ecosystems (Blair et al., 1985; Hagström et al., 1988; Henn and Chapela, 2000; Šantrůčková et al., 2000; Henn et al., 2002; Werth and Kuzyakov, 2010; Brüggemann et al., 2011; Dijkstra et al., 2011a,b; Penger et al., 2014).”
Background
The Metal-Dependent Regulators FurA and FurB from Mycobacterium Tuberculosis
Lucarelli, D., Vasil, M. L., Meyer‐Klaucke, W., & Pohl, E. (2008) · International Journal of Molecular Sciences · doi:10.3390/ijms9081548 · Cited by 28
“Accordingly, such members have now been named Zur [24], Nur [25] and Mur [26] which connotes that these family members are capable of selectively binding to a specific divalent transition metal other than Fe2+ to activate their DNA binding function.”
Influential
Complete Genome of Lactobacillus iners KY Using Flongle Provides Insight Into the Genetic Background of Optimal Adaption to Vaginal Econiche
Kwak, W., Han, Y.-H., Seol, D., Kim, H., Ahn, H., Jeong, M., Kang, J., Kim, H., & Kim, T. H. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01048 · Cited by 27
Bioinformatic and Expression Analyses of Genes Mediating Zinc Homeostasis inNostoc punctiforme
Hudek, L., Rai, L. C., Freestone, D., Michalczyk, A. A., Gibson, M., Song, Y., & Ackland, M. L. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02481-08 · Cited by 27
“coli, this is an ATP-dependent, high-affinity uptake system that is repressed in the presence of 10 M Zn(2) through activation of a zinc uptake regulator (Zur) (35, 48).”
Background
Specific features of l-histidine production by Escherichia coli concerned with feedback control of AICAR formation and inorganic phosphate/metal transport
Malykh, E. A., Butov, I. A., Равчеева, А. Б., Krylov, A. A., Mashko, S. V., & Stoynova, N. V. (2018) · Microbial Cell Factories · doi:10.1186/s12934-018-0890-2 · Cited by 26
“To elucidate the roles of the other known Zn2+ transport systems during His production, we tested variants of a His-producing strain with a deleted znuA gene, which encodes the substrate-binding component of the ZnuABC high-affinity zinc uptake system [71], for His accumulation; the znuA deletion did not affect cell g…”
Method
Critical Role of Zur and SmtB in Zinc Homeostasis of Mycobacterium smegmatis
Goethe, E., Laarmann, K., Luehrs, J., Jarek, M., Meens, J., Lewin, A., & Goethe, R. (2020) · mSystems · doi:10.1128/msystems.00880-19 · Cited by 26
“The most prominent family of inducible high-afﬁnity bacterial zinc transporters is the common ATP binding cassette (ABC) importer ZnuABC, which is an important virulence factor in many bacteria, e.g., E. coli , Salmonella enterica , Campylobacter jejuni , and Yersinia pestis (14–19).”
In vivo bioluminescence imaging of Escherichia coli O104:H4 and role of aerobactin during colonization of a mouse model of infection
Torres, A. G., Cieza, R. J., Rojas-López, M., Blumentritt, C. A., Souza, C. S., Johnston, R., Strockbine, N., Kaper, J. B., Sbrana, E., & Popov, V. L. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-112 · Cited by 27
“MacConkey agar is considered a low iron-containing medium which has been used to identify high-affinity iron and zinc uptake systems [25].”
Background
The Zinc Nutritional Immunity of Epinephelus coioides Contributes to the Importance of znuC During Pseudomonas plecoglossicida Infection
Huang, L., Zuo, Y., Qin, Y., Zhao, L., Lin, M., & Yan, Q. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.678699 · Cited by 26
“coli are transcribed into a single mRNA molecule (74).”
Background
Absence of ZnuABC-mediated zinc uptake affects virulence-associated phenotypes of uropathogenicEscherichia coli CFT073 under Zn(II)-depleted conditions
Gunasekera, T. S., Herre, A. H., & Crowder, M. W. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2009.01762.x · Cited by 26
Iron Acquisition in Mycobacterium avium subsp. paratuberculosis
Wang, J., Moolji, J., Dufort, A., Staffa, A., Domenech, P., Reed, M. B., & Behr, M. A. (2015) · Journal of Bacteriology · doi:10.1128/jb.00922-15 · Cited by 25
“MAP3775c has a nucleotide-binding domain similar to that of ZnuC, the ATPase subunit of an ABC transporter, found in Escherichia coli (54, 56).”
The Components of the Unique Zur Regulon of Cupriavidus metallidurans Mediate Cytoplasmic Zinc Handling
Bütof, L., Schmidt-Vogler, C., Herzberg, M., Große, C., & Nies, D. H. (2017) · Journal of Bacteriology · doi:10.1128/jb.00372-17 · Cited by 25
“1) ZnuABC, which is controlled by the Zur regulator of the 80 Fur protein family (12-15).”
Background
Interplay between copper and zinc homeostasis through the transcriptional regulator Zur in Enterococcus faecalis
Latorre, M., Low, M., Gárate, E., Reyes-Jara, A., Murray, B. E., Cambiazo, V., & González, M. (2015) · Metallomics · doi:10.1039/c5mt00043b · Cited by 25
Control of zinc homeostasis in Agrobacterium tumefaciens via zur and the zinc uptake genes znuABC and zinT
Bhubhanil, S., Sittipo, P., Chaoprasid, P., Nookabkaew, S., Sukchawalit, R., & Mongkolsuk, S. (2014) · Microbiology · doi:10.1099/mic.0.082446-0 · Cited by 25
Structure and electrostatic property of cytoplasmic domain of ZntB transporter
Tan, K., Sather, A., Robertson, J., Moy, S. F., Roux, B., & Joachimiak, A. (2009) · Protein Science · doi:10.1002/pro.215 · Cited by 24
Identification, Functional Characterization, and Regulon Prediction of the Zinc Uptake Regulator (zur) of Bacillus anthracis – An Insight Into the Zinc Homeostasis of the Pathogen
Kandari, D., Gopalani, M., Gupta, M. K., Joshi, H., Bhatnagar, S., & Bhatnagar, R. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03314 · Cited by 25
“coli as an SBP of a high-affinity zinc acquisition system ZnuABC, binds to the Zn+2 ions, facilitating its transportation across the membrane (Patzer and Hantke, 1998).”
BackgroundInfluential
An overview ofSalmonella entericametal homeostasis pathways during infection
Cunrath, O., & Palmer, J. D. (2021) · microLife · doi:10.1093/femsml/uqab001 · Cited by 25
“Molybdate is thought to enter the periplasm by diffusion through porins, where it is then transported through the inner membrane by the ABC transporter ModABC, in which ModA is the periplasmic binding protein, ModB the permease and ModC the ATPase (Walkenhorst et al. 1995) (Fig.”
BackgroundInfluential
How Zinc-Binding Systems, Expressed by Human Pathogens, Acquire Zinc from the Colonized Host Environment: A Critical Review on Zincophores
Remelli, M., Bellotti, D., & Rowińska‐Żyrek, M. (2021) · Current Medicinal Chemistry · doi:10.2174/1389200222666210514012945 · Cited by 25
Roles of Agrobacterium tumefaciens C58 ZntA and ZntB and the transcriptional regulator ZntR in controlling Cd2+/Zn2+/Co2+ resistance and the peroxide stress response
Chaoprasid, P., Nookabkaew, S., Sukchawalit, R., & Mongkolsuk, S. (2015) · Microbiology · doi:10.1099/mic.0.000135 · Cited by 26
Investigation of the role of ZurR in the physiology and pathogenesis of Listeria monocytogenes
Dowd, G. C., Casey, P. G., Begley, M., Hill, C., & Gahan, C. G. M. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2011.02472.x · Cited by 24
“It is necessary for almost all living organisms as it acts as both structural and catalytic cofactors in numerous enzymes and proteins (Patzer & Hantke, 1998).”
Background
Metal Ion Homeostasis in Listeria monocytogenes and Importance in Host–Pathogen Interactions
Jesse, H. E., Roberts, I. S., & Cavet, J. S. (2014) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/bs.ampbs.2014.08.003 · Cited by 24
Optimization of industrial microorganisms: recent advances in synthetic dynamic regulators
Min, B. E., Hwang, H. G., Lim, H. G., & Jung, G. Y. (2016) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-016-1867-y · Cited by 24
Transport of Metals: A Key Process in Oxygenic Photosynthesis
Pakrasi, H. B., Ogawa, T., & Bhattacharyya‐Pakrasi, M. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-48148-0_14 · Cited by 24
“Significant among these studies are two recent reports from Patzer and Hantke ( Patzer and Hantke, 1998; Patzer and Hantke, 2000) who have identified an ABC-type Zn-permease in E. coli.”
Result
Mechanisms and Regulation of Iron Homeostasis in the Rhizobia
Fabiano, E., & O’Brian, M. R. (2012) · Springer briefs in molecular science · doi:10.1007/978-94-007-5267-2_3 · Cited by 22
“Fur is the founding member of a family of regulators which also includes Zur (Gaballa and Helmann 1998; Patzer and Hantke 1998), PerR (Bsat et al.”
Background
Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-l-homocysteine hydrolase from Pseudomonas aeruginosa
Czyrko, J., Śliwiak, J., Imiolczyk, B., Gdaniec, Z., Jaskólski, M., & Brzeziński, K. (2018) · Scientific Reports · doi:10.1038/s41598-018-29535-y · Cited by 24
Time-dependent translational response of E. coli to excess Zn(II).
Easton, J. A., Thompson, P. M., & Crowder, M. W. (2006) · PubMed Central · Cited by 23
Physiological and Genetic Aspects of Micronutrient Uptake by Higher Plants
Yang, X., & Römheld, V. (1999) · Springer eBooks · doi:10.1007/978-94-017-2685-6_20 · Cited by 23
The metabolism and morphology mutation response of probiotic Bacillus coagulans for lead stress
Xing, S.-C., Mi, J., Chen, J., Xiao, L., Wu, Y., Liang, J. B., Zhang, L., & Liao, X. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.07.296 · Cited by 22
Phenotypic profile linked to inhibition of the major Zn influx system in Salmonella enterica : proteomics and ionomics investigations
Ciavardelli, D., Ammendola, S., Ronci, M., Consalvo, A., Marzano, V., Lipoma, M., Sacchetta, P., Federici, G., Ilio, C. D., Battistoni, A., et al. (2010) · Molecular BioSystems · doi:10.1039/c0mb00140f · Cited by 22
Genome-wide identification of Bacillus subtilis Zur-binding sites associated with a Zur box expands its known regulatory network
Prestel, E., Noirot, P. H., & Auger, S. (2015) · BMC Microbiology · doi:10.1186/s12866-015-0345-4 · Cited by 23
“In the Gram positive bacterium Bacillus subtilis, transcription of genes involved in zinc homeostasis is regulated by Zur, a metalloprotein that binds Zn(II) as corepressor [6-9].”
Background
The ropAe gene encodes a porin‐like protein involved in copper transit in Rhizobium etli CFN42
González, A., Cubillas, C. A., Miranda, F., Dávalos, A., & Santos, A. G.-D. L. (2017) · MicrobiologyOpen · doi:10.1002/mbo3.573 · Cited by 22
“There are several examples cited in the literature of upregulation of high- affinity porin- encoding genes at lowmetal concentrations (Hohle & O’Brian, 2009; Patzer & Hantke, 1998; Speer et al., 2013).”
Candida albicans zincophore and zinc transporter interactions with Zn( ii ) and Ni( ii )
Łoboda, D., & Rowińska‐Żyrek, M. (2018) · Dalton Transactions · doi:10.1039/c7dt04403h · Cited by 22
Intracellular Accumulation of Staphylopine Can Sensitize Staphylococcus aureus to Host-Imposed Zinc Starvation by Chelation-Independent Toxicity
Grim, K. P., Radin, J. N., Solórzano, P. K. P., Morey, J. R., Frye, K. A., Ganio, K., Neville, S. L., McDevitt, C. A., & Kehl‐Fie, T. E. (2020) · Journal of Bacteriology · doi:10.1128/jb.00014-20 · Cited by 22

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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