Binding of the Fur (ferric uptake regulator) repressor of Escherichia coli to arrays of the GATAAT sequence
Abstract
The mode of DNA binding of the Fur (ferric uptake regulator) repressor which controls transcription of iron-responsive genes in Escherichia coli, has been re-examined. Using as a reference the known sites at the promoter of the aerobactin operon of Escherichia coli, we have compared in detail the patterns of interaction between the purified Fur protein and natural or synthetic DNA targets. DNase I and hydroxyl radical footprinting, as well as missing-T assays, consistently revealed that functional Fur sites are composed of a minimum of three repeats of the hexameric motif GATAAT rather than by a palindromic 19 bp target sequence. Extended binding sites, constructed by stepwise addition of one or two direct repeats of the same sequence, were occupied co-operatively by Fur with the same pattern of interactions as those observed with the core of three repeats. This indicated that functional sites with a range of affinities can be formed by the addition of discrete GATAAT extensions to a minimal recognition sequence. The fashion in which Fur binds its target, virtually unknown in prokaryotic transcriptional regulators, accounts for the observed helical wrapping of the protein around the DNA helix.
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The thymine base is an essential recognition element for direct contacts with Fur.
“Therefore, the thymine base is an essential recognition element for direct contacts with Fur.”
From Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator (2015) · cites this paper as [11]
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“…polarization (FP) experiments with Fur and Fur YdiV to test whether YdiV had any effect on the DNA-binding ability of Fur. Surprisingly, while the native Fur readily bound to the Fur box DNA (51), the co-expressed Fur YdiV protein did not form a complex with the Fur box DNA (Figure 2C).”
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- Authors
- Escolar, L., Pérez-Martı́n, J., & de Lorenzo, V.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1998-10
- Volume
- 283
- Issue
- 3
- Pages
- 537-547
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1986738890
- Cited by
- 173
- References
- 53
- Citations by year
- 2025: 1 · 2024: 4 · 2023: 3 · 2022: 3 · 2021: 5 · 2020: 6 · 2019: 3 · 2018: 4 · 2017: 8 · 2016: 6 · 2015: 8 · 2014: 6 · 2013: 5 · 2012: 9
- FWCI
- 4.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Diffusion and Search Dynamics
- Keywords
- Fur repressor, ferric uptake regulator, Escherichia coli, DNA binding, iron-responsive genes, transcriptional regulation, cooperative DNA binding, protein-DNA interactions, DNA footprinting
- MeSH terms
- Bacterial Proteins, Binding Sites, DNA-Binding Proteins, DNA, Bacterial, Escherichia coli, Iron, Promoter Regions, Genetic, Repetitive Sequences, Nucleic Acid, Repressor Proteins, Gene Expression Regulation, Bacterial, DNA Footprinting
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