The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
The ZnuABC high‐affinity zinc uptake system and its regulator Zur in Escherichia coli
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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. R., Plunkett, G., Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado‐Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., et al. (1997) · Science · doi:10.1126/science.277.5331.1453 · Cited by 7,609
Chang, A. C. Y., & Cohen, S. N. (1978) · Journal of Bacteriology · doi:10.1128/jb.134.3.1141-1156.1978 · Cited by 4,261
Tabor, S., & Richardson, C. C. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.4.1074 · Cited by 3,165
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
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.
Cited by
Sorted by citations
Items 301–400 of 490
Takahashi, H., Oshima, T., Hobman, J. L., Doherty, N., Clayton, S., Iqbal, M., Hill, P. J., Tobe, T., Ogasawara, N., Kanaya, S., et al. (2015) · Journal of The Royal Society Interface · doi:10.1098/rsif.2015.0069 · Cited by 22
“The highest activity of the znuCB promoter (PznuCB) was seen in the Dzur strain, concordant with Zur being a repressor of znuABC expression [5].”
BackgroundAn, R., Sreevatsan, S., & Grewal, P. S. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-433 · Cited by 22
“temperata, pchC, a gene involved in the biogenesis of pyochelin type of siderophore [61], was upregulated indicating the importance of iron, whereas a siderophore-independent zinc ion transport system encoded by gene znuA [62] was induced in X.”
BackgroundSarvan, S., Charih, F., Askoura, M., Butcher, J., Brunzelle, J. S., Stintzi, A., & Couture, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-25157-6 · Cited by 21
Wang, P., Yu, Z., Santangelo, T. J., Olesik, J. W., Wang, Y., Heldwein, E. E. Z., & Li, X. (2017) · Journal of Bacteriology · doi:10.1128/jb.00276-17 · Cited by 21
Bellotti, D., Rowińska‐Żyrek, M., & Remelli, M. (2020) · Dalton Transactions · doi:10.1039/d0dt01626h · Cited by 20
A critical role of the periplasm in copper homeostasis in Gram-negative bacteria
Ishihara, J.-I., Mekubo, T., Kusaka, C., Kondo, S., Oiko, R., Igarashi, K., Aiba, H., Ishikawa, S., Ogasawara, N., Oshima, T., et al. (2020) · Biosystems · doi:10.1016/j.biosystems.2023.104980 · Cited by 20
Metagenomic insights into the prokaryotic communities of heavy metal-contaminated hypersaline soils
Galisteo, C., Puente‐Sánchez, F., de la Haba, R. R., Bertilsson, S., Sánchez‐Porro, C., & Ventosa, A. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.175497 · Cited by 21
ΔznuAΔpurE Brucella abortus 2308 mutant as a live vaccine candidate
Yang, X., Thornburg, T., Walters, N., & Pascual, D. W. (2009) · Vaccine · doi:10.1016/j.vaccine.2009.10.113 · Cited by 20
Graham, A. I., Sanguinetti, G., Bramall, N., McLeod, C. W., & Poole, R. K. (2011) · Microbiology · doi:10.1099/mic.0.053843-0 · Cited by 22
“ZnuA forms the soluble periplasmic metallochaperone that captures and delivers Zn to ZnuBC, the membrane-bound component of the highaffinity Zn importer (Patzer & Hantke, 1998; Patzer & Hantke, 2000).”
BackgroundWarner, D. M., & Levy, S. B. (2011) · Journal of Bacteriology · doi:10.1128/jb.05451-11 · Cited by 20
“divergently transcribed znuCB genes (38) (Fig.”
Yang, X., Clapp, B., Thornburg, T., Hoffman, C. A., & Pascual, D. W. (2016) · Vaccine · doi:10.1016/j.vaccine.2016.09.004 · Cited by 20
“The znuA gene encodes a high affinity-binding protein that is a key cofactor at acquiring Zn2+ from phagosomes [33], which is required for the activity of Cu, Zn superoxide dismutase enabling Brucella to resist oxidative stress [34].”
BackgroundAbreu, I., Mihelj, P., & Raimunda, D. (2019) · Metallomics · doi:10.1039/c8mt00372f · Cited by 21
McQuillan, J. S., & Shaw, A. M. (2013) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2013.07.024 · Cited by 19
The Different Types of Metallophores Produced by Salmonella enterica: A Review
Mohsen, Y., Tarchichi, N., Barakat, R., Kawtharani, I., Ghandour, R., Ezzeddine, Z., & Ghssein, G. (2023) · Microbiology Research · doi:10.3390/microbiolres14030099 · Cited by 19
Zinc, Cadmium, and Lead Resistance and Homeostasis
Rensing, C., & Mitra, B. (2007) · Springer eBooks · doi:10.1007/7171_2006_083 · Cited by 19
“The ZnuABC complex catalyzes ATP-dependent uptake of zinc (Patzer and Hantke 1998).”
BackgroundRole of a Fur homolog in iron metabolism in Nitrosomonas europaea
Vajrala, N., Sayavedra‐Soto, L. A., Bottomley, P. J., & Arp, D. J. (2011) · BMC Microbiology · doi:10.1186/1471-2180-11-37 · Cited by 19
“coli [15] has two, Bacillus subtilis [16], Mycobacterium smegmatis have three, Staphylococcus aureus and some species of Brucella have four and Thermoanaerobacter tengcongensis has five fur homologs [17].”
BackgroundEckelt, E., Jarek, M., Frömke, C., Meens, J., & Goethe, R. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-1076 · Cited by 19
“coli [51,52] and Salmonella Typhimurium [53].”
Interplay between the Zur Regulon Components and Metal Resistance in Cupriavidus metallidurans
Bütof, L., Große, C., Lilie, H., Herzberg, M., & Nies, D. H. (2019) · Journal of Bacteriology · doi:10.1128/jb.00192-19 · Cited by 19
“In Escherichia coli, the Zinc uptake regulator Zur, a member of the Fur family of regulators, controls expression of znuABC for high-specificity import of zinc ions (26, 27).”
BackgroundIron homeostasis of cyanobacteria: advancements in siderophores and metal transporters
Fresenborg, L., Graf, J., Schätzle, H., & Schleiff, E. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819311-2.00007-3 · Cited by 19
Structural basis for zinc-induced activation of a zinc uptake transcriptional regulator
Liu, F., Su, Z., Chen, P., Tian, X., Wu, L., Tang, D., Li, P., Deng, H., Ding, P., Fu, Q., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab432 · Cited by 19
“…to its critical role in regulation of zinc homeostasis, Zur homologs have been identified in a number of bacteria, including Escherichia coli (10), Bacillus subtilis (11), Listeria monocytogenes (12), Staphylococcus aureus (13), Xanthomonas campestris (8), Mycobacterium tuberculosis (14),…”
Comparative Genomics Analysis of the Metallomes
Gladyshev, V. N., & Zhang, Y. (2012) · Metal ions in life sciences · doi:10.1007/978-94-007-5561-1_16 · Cited by 21
Understanding How Cells Allocate Metals
Tottey, S., Harvie, D. R., & Robinson, N. J. (2007) · Springer eBooks · doi:10.1007/7171_2006_072 · Cited by 19
Nitric oxide releases intracellular zinc from prokaryotic metallothionein in Escherichia coli
Binet, M. R. B., Cruz-Ramos, H., Laver, J. R., Hughes, M., & Poole, R. K. (2002) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2002.tb11295.x · Cited by 19
Ossa, F. O., Pons, M., Bekker, A., Hofmann, A., Poulton, S. W., Andersen, M. B., Agangi, A., Gregory, D. D., Reinke, C., Steinhilber, B., et al. (2023) · Earth and Planetary Science Letters · doi:10.1016/j.epsl.2023.118147 · Cited by 19
The Tricky Ways Bacteria Cope with Iron Limitation
Braun, V., & Hantke, K. (2013) · Springer briefs in molecular science · doi:10.1007/978-94-007-6088-2_2 · Cited by 18
Self-citationJaggavarapu, S., & O’Brian, M. R. (2014) · Molecular Microbiology · doi:10.1111/mmi.12584 · Cited by 18
“It is also at variance with findings for essentially all other characterized Fur family proteins, where in those cases the protein-binding regulatory ligand greatly diminishes DNA binding activity (Bsat et al., 1998; Gaballa and Helmann, 1998; Patzer and Hantke, 1998; Ahn et al., 2006; Platero et al., 2007; Hohle and…”
BackgroundResultGrover, A., & Sharma, R. (2006) · Journal of Bacteriology · doi:10.1128/jb.00643-06 · Cited by 18
“TPEN addition to culture medium at a final concentration of 1.0 M was able to reduce promoter activity about threefold, whereas further additions of TPEN of up to 7.5 M did not reduce expression of the gene below a basal -galactosidase activity of 170.10 5.30 U/mg protein (Fig.”
InfluentialSpus, M., Liu, H., Wels, M., Abee, T., & Smid, E. J. (2016) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2016.10.020 · Cited by 19
“We found another SNP in the homologue of znuB in E. coli (Patzer and Hantke, 1998), encoding the membrane-embedded protein of an ABC-type Mn2+/Zn2+ transport system.”
BackgroundBiphasic unbinding of a metalloregulator from DNA for transcription (de)repression in Live Bacteria
Jung, W., Sengupta, K., Wendel, B. M., Helmann, J. D., & Chen, P. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa056 · Cited by 17
Hantke, K. (2014) · ASM Press eBooks · doi:10.1128/9781555816544.ch12 · Cited by 18
Self-citationHecel, A., Kola, A., Valensin, D., Kozłowski, H., & Rowińska‐Żyrek, M. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b03298 · Cited by 17
Yuan, F., Liao, Y., You, W., Liu, Z., Tan, Y., Zheng, C., BinWang, Zhou, D., Tian, Y., & Bei, W. (2014) · Veterinary Microbiology · doi:10.1016/j.vetmic.2014.10.016 · Cited by 17
Transition metals and host-microbe interactions in the inflamed intestine
Zhu, W., Spiga, L., & Winter, S. (2019) · BioMetals · doi:10.1007/s10534-019-00182-8 · Cited by 17
Randazzo, P., Anba‐Mondoloni, J., Aubert-Frambourg, A., Guillot, A., Péchoux, C., Vidić, J., & Auger, S. (2019) · Journal of Bacteriology · doi:10.1128/jb.00547-19 · Cited by 18
Physiological and Genetic Aspects of Crop Plant Adaptation to Elemental Stresses in Acid Soils
Yang, X., Wang, W., Ye, Z., He, Z. L., & Baligar, V. C. (2004) · Springer eBooks · doi:10.1007/978-1-4020-2138-1_13 · Cited by 18
Teramoto, H., Inui, M., & Yukawa, H. (2012) · FEBS Journal · doi:10.1111/febs.12028 · Cited by 17
The Bradyrhizobium japonicum Fur protein is an iron-responsive regulator in vivo
Yang, J., Sangwan, I., & O’Brian, M. R. (2006) · Molecular Genetics and Genomics · doi:10.1007/s00438-006-0162-4 · Cited by 17
“Fur is the founding member of a family of metal-dependent regulators, including Zur (Gaballa and Helmann 1998; Patzer and Hantke 1998; Gaballa et al. 2002), Mur (Chao et al. 2004; Diaz-Mireles et al. 2004; Platero et al. 2004), Nur (Ahn et al. 2006), PerR (Bsat et al. 1998; Horsburgh et al. 2002), and Irr (Hamza et al…”
BackgroundMetal Metabolism and Toxicity: Repetitive DNA
Robinson, N. J., Rutherford, J. C., Pocock, M. R., & Cavet, J. S. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46855-7_16 · Cited by 17
Zinc Oxide Nanoparticles Induce Cell Filamentation in Escherichia coli
Gunawan, C., Teoh, W. Y., Ricardo, Marquis, C. P., & Amal, R. (2013) · Particle & Particle Systems Characterization · doi:10.1002/ppsc.201200152 · Cited by 16
The hierarchic network of metal-response transcription factors in Escherichia coli
Yamamoto, K. (2014) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2014.915731 · Cited by 16
Li, K., Gifford, A. H., Hampton, T. H., & O’Toole, G. A. (2019) · Journal of Bacteriology · doi:10.1128/jb.00618-19 · Cited by 18
“ZnuABC is a member of the 80 ATP-binding cassette (ABC) transporters, consisting of a zinc-specific binding periplasmic 81 protein (ZnuA), an inner membrane permease (ZnuB), and an ATPase (ZnuC) (35, 37, 40).”
BackgroundCastelli, S., Stella, L., Petrarca, P., Battistoni, A., Desideri, A., & Falconi, M. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.11.073 · Cited by 15
“In particular, it has been established that several bacteria respond to zinc deficiency by expressing the ZnuABC high affinity zinc uptake system, a transporter of the ABC family whose expression is repressed by the metallated form of the regulatory protein Zur [4].”
BackgroundYu, Y., Su, J., Xu, J., Li, Y. P., Alwathnani, H. A., Wu, Z., Ji, C., Feng, R., Rensing, C., & Herzberg, M. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.00312-22 · Cited by 15
“subtilis, the induction of znuABC (54) and yciC has been suggested to constitute the second phase or wave in response to zinc deprivation.”
BackgroundHussein, K. A., & Joo, J. H. (2017) · Rhizosphere · doi:10.1016/j.rhisph.2017.05.006 · Cited by 15
Hohle, T. H., & O’Brian, M. R. (2016) · Molecular Microbiology · doi:10.1111/mmi.13381 · Cited by 16
“…regulators sense and respond to the cellular status of a specific divalent metal to regulate genes under their control (Ahn et al., 2006; Bsat et al., 1998; Chao et al., 2004; Diaz-Mireles et al., 2004; Gaballa and Helmann, 1998; Hamza et al., 1998; Patzer and Hantke, 1998; Platero et al., 2004).”
BackgroundZinc is an inhibitor of the LdtR transcriptional activator
Pagliai, F. A., Pan, L., da Silva, D. R. P., González, C. F., & Lorca, G. L. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195746 · Cited by 14
A flow equilibrium of zinc in cells of Cupriavidus metallidurans
Nies, D. H., Schleuder, G., Galea, D., & Herzberg, M. (2024) · Journal of Bacteriology · doi:10.1128/jb.00080-24 · Cited by 14
“A.1) zinc importer such as ZnuABC from E. coli (25, 27, 31, 32) so ZupT is an important zinc importer in this bacterium.”
BackgroundCo(ii)-detection does not follow Kco(ii) gradient: channelling in Co(ii)-sensing
Patterson, C. J., Pernil, R., Dainty, S. J., Chakrabarti, B., Henry, C. E., Money, V. A., Foster, A. W., & Robinson, N. J. (2013) · Metallomics · doi:10.1039/c3mt20241k · Cited by 14
Molecular Mechanisms of Phosphate Homeostasis in Escherichia coli
McCleary, W. R. (2017) · InTech eBooks · doi:10.5772/67283 · Cited by 14
“However, considering the homologies between PitA and PitB with other Pi transporters from other organisms, it seems unlikely that they are retained in this genome primarily to function as transporters of divalent metal cations, which have their own primary transporters, as well [36].”
BackgroundStructure and Metal Binding Properties of Chlamydia trachomatis YtgA
Luo, Z., Neville, S. L., Campbell, R., Morey, J. R., Menon, S., Thomas, M., Eijkelkamp, B. A., Ween, M. P., Huston, W. M., Kobe, B., et al. (2019) · Journal of Bacteriology · doi:10.1128/jb.00580-19 · Cited by 14
“The sequences of the 32 SBPs included in this study were obtained from the NCBI under the following GI accession numbers: Bacillus anthracis MntA, GI:229264967 (61); Bacillus subtilis YcdH, GI:2415736 (62); Bacillus subtilis YclQ, GI:758317765 (63); Campylobacter jejuni ZnuA, GI:384442496 (64); Chlamydia trachomatis Y…”
MethodA Galvanizing Story—Protein Stability and Zinc Homeostasis
Chivers, P. T. (2007) · Journal of Bacteriology · doi:10.1128/jb.00173-07 · Cited by 14
“Zinc ions are transported into the cytoplasm via ZnuABC (14), although other import pathways exist (5).”
BackgroundInfluentialRasmussen, R. A., Wang, S., Camarillo, J. M., Sosnowski, T., Cho, B.-K., Goo, Y. A., Lucks, J. B., & O’Halloran, T. V. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1086 · Cited by 13
“coli genes, we next sought to determine if L31-sfGFP protein levels were also affected by exogenous zinc concentration in the media (20,46).”
BackgroundSpecific Zn(II)-binding site in the C-terminus of Aspf2, a zincophore from Aspergillus fumigatus
Garstka, K., Hecel, A., Kozłowski, H., & Rowińska‐Żyrek, M. (2022) · Metallomics · doi:10.1093/mtomcs/mfac042 · Cited by 12
Braz, V. S., Neto, J. F. D. S., Italiani, V. C. S., & Marques, M. V. (2010) · Journal of Bacteriology · doi:10.1128/jb.00496-10 · Cited by 13
“In Escherichia coli, zinc uptake is performed mainly by ABC transporters, such as the high-affinity system ZnuABC (26), but other systems also contribute, such as the low-affinity zinc-phosphate cotransporter Pit (2) and the broad-spectrum substrate transporter ZupT (9), both of which work when there are medium levels…”
BackgroundHermansen, G. M. M., Hansen, M. L., Khademi, S. M. H., & Jelsbak, L. (2018) · Microbiology · doi:10.1099/mic.0.000687 · Cited by 13
Kelley, B. R., Lu, J., Haley, K. P., Gaddy, J. A., & Johnson, J. G. (2020) · Metallomics · doi:10.1093/mtomcs/mfaa002 · Cited by 12
Zinc acquisition and its contribution to Klebsiella pneumoniae virulence
Maunders, E. A., Giles, M. W., Ganio, K., Cunningham, B. A., Bennett-Wood, V. R., Cole, G. B., Ng, D., Lai, C. C.-L., Neville, S. L., Moraes, T. F., et al. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1322973 · Cited by 12
“In the Enterobacteriaceae, the prototypical example of this pathway is ZnuCBA from E. coli (Patzer and Hantke, 1998; Ammendola et al., 2007).”
BackgroundMethodOsmotic stress induces long-term biofilm survival in Liberibacter crescens
Padgett‐Pagliai, K. A., Pagliai, F. A., da Silva, D. R. P., Gardner, C. L., Lorca, G. L., & González, C. F. (2022) · BMC Microbiology · doi:10.1186/s12866-022-02453-w · Cited by 12
Crystal structure of E. coli ZinT with one zinc-binding mode and complexed with citrate
Chen, J., Wang, L., Shang, F., Dong, Y., Ha, N., Nam, K. H., Quan, C., & Xu, Y. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.03.192 · Cited by 12
The ancient alarmone ZTP and zinc homeostasis in Bacillus subtilis
Nies, D. H. (2019) · Molecular Microbiology · doi:10.1111/mmi.14332 · Cited by 12
“COG0523 members are often encoded as part of the zinc-starvation response gene clusters, which are expressed under control of the zinc uptake regulator Zur (Patzer and Hantke, 1998; Patzer and Hantke, 2000; Hantke, 2005; Haas et al., 2009), as is the YciC protein in B.”
BackgroundBacterial zinc transporters and regulators
Hantke, K. (2001) · Springer eBooks · doi:10.1007/978-94-017-3728-9_4 · Cited by 12
Self-citationChen, J., Wang, L., Li, W., Zheng, X. S., & Li, X. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.784575 · Cited by 10
“…54 heavy metal-related genes (Figure 2), including potential metal resistance genes homologous to zntA of E. coli, czcD of C. metallidurans, copAB of Legionella pneumophila (Purohit et al., 2018), cutC of Enterococcus faecalis (Latorre et al., 2011), znuA of E. coli (Patzer and Hantke, 1998), etc.”
BackgroundSalam, L. B. (2022) · Folia Microbiologica · doi:10.1007/s12223-022-00970-9 · Cited by 11
“…of resistance genes involved in the transport of zinc and other divalent cations (zupT (Zn/Fe/Co/ Ni/Cu/Cd)), high-affinity zinc transporter znuC (Patzer and Hantke 1998), nickel (nikA, nikB), molybdenum (modA, modB, modC, modE), magnesium (mgtA, corA, corC, corD (Co/Mg)), and genes for efflux…”
BackgroundIron and Zinc Regulate Expression of a Putative ABC Metal Transporter in Corynebacterium diphtheriae
Peng, E. D., Oram, D. M., Battistel, M. D., Lyman, L. R., Freedberg, D. I., & Schmitt, M. P. (2018) · Journal of Bacteriology · doi:10.1128/jb.00051-18 · Cited by 11
Luna‐Bulbarela, A., Romero-Gutiérrez, T., Tinoco‐Valencia, R., Ortíz, E., Martínez-Romero, M. E., Galindo, E., & Serrano‐Carreón, L. (2023) · Microbiological Research · doi:10.1016/j.micres.2023.127592 · Cited by 10
Activation of zinc uptake regulator by zinc binding to three regulatory sites
Choi, Y., Koh, J., Cha, S., & Roe, J. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae079 · Cited by 11
“Since its discovery in Esc heric hia coli and Bacillus subtilis ( 15 ,16 ), it has been found in > 2600 different species of bacteria ( 17 ).”
BackgroundThe Escherichia coli AZY operon links copper uptake to antibiotic resistance
Palmer, C. D., Ghnamah, Y., Livnat‐Levanon, N., Lewinson, O., & Rosenzweig, A. C. (2025) · Communications Biology · doi:10.1038/s42003-025-07884-5 · Cited by 10
Behrendt, L., Raina, J., Lutz, A., Kot, W., Albertsen, M., Nielsen, P. H., Sørensen, S. J., Larkum, A. W. D., & Kühl, M. (2017) · The ISME Journal · doi:10.1038/ismej.2017.192 · Cited by 10
Houdt, R. V., Vandecraen, J., Leys, N., Monsieurs, P., & Aertsen, A. (2021) · Microorganisms · doi:10.3390/microorganisms9020309 · Cited by 10
“metallidurans strains do not contain a high-affinity zinc uptake system like the ATPbinding cassette (ABC) uptake system ZnuABC from Escherichia coli [20].”
BackgroundWang, T., Yang, X., Gao, F., Zhao, C., Kang, Y., Wang, Y., & Shen, X. (2016) · Annals of Microbiology · doi:10.1007/s13213-016-1205-7 · Cited by 10
Zinc Starvation Response in a Cyanobacterium Revealed
Nies, D. H. (2012) · Journal of Bacteriology · doi:10.1128/jb.00257-12 · Cited by 10
“Fur binds to its operators probably with iron as the corepressor and is the archetype of the Fur protein family of regulators that comprises, for instance, Nur for nickel, Mur for manganese, PerR for oxidative stress (20), and Zur for zinc (15, 46).”
BackgroundInfluentialUnraveling the genetic basis of microbial metal resistance: Shift from Mendelian to systems biology
Li, X., Basak, B., Tanpure, R. S., Zheng, X., & Jeon, B. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.138350 · Cited by 9
Salam, L. B. (2023) · Folia Microbiologica · doi:10.1007/s12223-023-01077-5 · Cited by 9
“…( zupT (Zn/Fe/Co/Ni/Cu/Cd), zipB (Zn/ Cd) (Fox and Guerinot 1998), psaB, psaC (Mn/Zn) (Novak et al. 1998), high-affinity zinc transporter znuABC (Patzer and Hantke 1998), mntABC (Mn), nickel/cobalt (nickel ABC transporter nikB, nikD, nikE, nikV, nikW, cbiO, and several others),…”
Schulz, V., Galea, D., Herzberg, M., & Nies, D. H. (2024) · Journal of Bacteriology · doi:10.1128/jb.00395-23 · Cited by 9
Bacterial-nanoparticle interactions
McQuillan, J. S. (2010) · UPT. Syiah Kuala University Library (Syiah Kuala University) · Cited by 9
Singh, A., & Kumawat, K. C. (2025) · Journal of Agriculture and Food Research · doi:10.1016/j.jafr.2025.101832 · Cited by 8
Characterization of the Zinc Uptake Repressor (Zur) from Acinetobacter baumannii
Kim, M., Le, M. T., Fan, L., Campbell, C., Sen, S., Capdevila, D. A., Stemmler, T. L., & Giedroc, D. P. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00679 · Cited by 8
Liu, M., Xu, W., Zhu, Y., Cui, X., & Pang, X. (2021) · Current Microbiology · doi:10.1007/s00284-021-02633-3 · Cited by 8
Identifying Neighborhoods of Coordinated Gene Expression and Metabolite Profiles
Hancock, T., Wicker, N., Takigawa, I., & Mamitsuka, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031345 · Cited by 8
“ions cofactors and is correlated with Cu, Mn, Ni and Co ions abundance”
Tierrafría, V. H., Mejía-Almonte, C., Camacho-Zaragoza, J. M., Salgado, H., Alquicira, K., Ishida, C., Gama‐Castro, S., & Collado‐Vides, J. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty689 · Cited by 8
How is a Zinc Ion Correctly Allocated to a Zinc-dependent Protein?
Nies, D. H. (2022) · Advances in environmental microbiology · doi:10.1007/978-3-030-97185-4_19 · Cited by 8
Ellison, M. L., Farrow, J. M., Parrish, W., Danell, A. S., & Pesci, E. C. (2013) · PLoS ONE · doi:10.1371/annotation/40be2093-f3d0-41ca-a8d7-02fecd051942 · Cited by 9
Bidzhieva, S. K., Tourova, T. P., Kadnikov, V. V., Samigullina, S. R., Sokolova, D. S., Poltaraus, A. B., Avtukh, A. N., Tereshina, V. M., Beletsky, A. V., Mardanov, A. V., et al. (2024) · Biology · doi:10.3390/biology13100800 · Cited by 7
“In the genome of strain 5S69 T , the znuABC genes (V8V93_05370, 08285–08290) were annotated, encoding a high-affinity transporter specialized for transporting zinc ions as part of a system for metal ion homeostasis in bacteria [82].”
BackgroundBilitewski, U., Blodgett, J. A. V., Duhme‐Klair, A., Dallavalle, S., Laschat, S., Routledge, A., & Schobert, R. (2017) · Angewandte Chemie · doi:10.1002/ange.201701586 · Cited by 7
Resistance to Metals Used in Agricultural Production
Rensing, C., Moodley, A., Cavaco, L. M., & McDevitt, S. F. (2018) · ASM Press eBooks · doi:10.1128/9781555819804.ch5 · Cited by 7
Liu, Y., Li, W., Wei, Y., Jiang, Y., & Tan, X. (2013) · Metallomics · doi:10.1039/c3mt00163f · Cited by 7
Microbe-Mediated Removal of Heavy Metals for Sustainable Agricultural Practices
Mallick, I., Ghosh, A. S., & Ghosh, A. (2019) · Soil biology · doi:10.1007/978-3-030-18933-4_24 · Cited by 7
Simulating in vitro transcriptional response of zinc homeostasis system in Escherichia coli
Cui, J., Kaandorp, J. A., & Lloyd, C. M. (2008) · BMC Systems Biology · doi:10.1186/1752-0509-2-89 · Cited by 7
“The genes znuA and znuCB are transcribed divergently and both promoters of znuA and znuCB are active in vivo [7,22].”
BackgroundInfluentialPaterson, J. R., Wadsworth, J. M., Hu, P., & Sharples, G. J. (2023) · Microbial Genomics · doi:10.1099/mgen.0.001153 · Cited by 6
“[58], mntS by MntR bound to Mn 2+ [72] and znuA by Zur bound to Zn 2+ [73].”
BackgroundGoethe, E., Gieseke, A., Laarmann, K., Luehrs, J., & Goethe, R. (2021) · Journal of Bacteriology · doi:10.1128/jb.00049-21 · Cited by 6
Resistance to Metals Used in Agricultural Production
Hasman, H., Franke, S., & Rensing, C. (2019) · ASM Press eBooks · doi:10.1128/9781555817534.ch7 · Cited by 6
Metals in Cells: Control of Cellular Metal Concentration
Gilston, B. A., & O’Halloran, T. V. (2004) · Wiley eBooks · doi:10.1002/9781119951438.eibc2107 · Cited by 6
Han, J., Han, X., Chen, Z., Xu, J., Zhang, W., Gu, Y., Peng, Y., Han, J., Xu, L., Shen, X., et al. (2025) · Stress Biology · doi:10.1007/s44154-025-00224-x · Cited by 5
“Previous research has demonstrated that Zur negatively regulates the zinc uptake transportor gene cluster, znu-ABC , to maintain zinc homeostasis in vivo (Patzer and Hantke 1998).”
Metabolic Responses, Uptake, and Export of Copper in Cyanobacteria
Oder, J. C., Sateles, T. E., de Souza, L. B., Nunes‐Nesi, A., Araújo, W. L., & Alvarenga‐Lucius, L. (2025) · Biology · doi:10.3390/biology14070798 · Cited by 5
“The transfer of Cu 2+ from ZnuA to the membrane permease ZnuB is necessary for its translocation into the cytosol, while the ATPase subunit ZnuC supplies the energy required for active transport [55].”
A ‘through-DNA’ mechanism for co-regulation of metal uptake and efflux
Chakraborty, U. K., Park, Y., Sengupta, K., Jung, W. J., Joshi, C. P., Francis, D. H., & Chen, P. (2024) · Nature Communications · doi:10.1038/s41467-024-55017-z · Cited by 5
Bacterial cell wall research in Tübingen: A brief historical account
Braun, V. (2014) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2014.12.013 · Cited by 5
A bioinformatic analysis of zinc transporters in intestinal Lactobacillaceae
Huynh, U., Nguyen, H. N., Trinh, B. K., Elhaj, J., & Zastrow, M. L. (2023) · Metallomics · doi:10.1093/mtomcs/mfad044 · Cited by 5
Wang, J., Capdevila, D. A., & Giedroc, D. P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14675-x · Cited by 5
Family matters: gene regulation by metal-dependent transcription factors
van Bakel, H., & Wijmenga, C. (2005) · Topics in current genetics · doi:10.1007/4735_104 · Cited by 5
Bosc, L., Sécher, T., Ball, G., Pennec, D. L., Tribout, M., Ba, M., Bai, Y., Ouerdane, L., Arnoux, P., Denis, Y., et al. (2026) · Infection and Immunity · doi:10.1128/iai.00453-25 · Cited by 5
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
