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.
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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]
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]
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Metal homeostasis and resistance in bacteria
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Self-citation
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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