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Review
. 2009 Jul;77(7):2590-601.
doi: 10.1128/IAI.00116-09. Epub 2009 Apr 13.

This is not your mother's repressor: the complex role of fur in pathogenesis

Affiliations
Review

This is not your mother's repressor: the complex role of fur in pathogenesis

Beth M Carpenter et al. Infect Immun. 2009 Jul.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Basic features of Fe-Fur repression, apo-Fur repression, and Fur activation. Characteristic features of each type of Fur regulation are shown as they interact with a target DNA promoter. (Left) Classical iron-bound Fur repression. As iron becomes increasingly available in the bacterial cell, the Fe(II) cofactor binds to apo-Fur monomers, and these now-iron-bound monomers dimerize. The iron-bound Fur dimers repress transcription by binding to the Fur box in their target promoters and block the binding of RNA polymerase. (Center) Iron-bound Fur and apo-Fur activation. On the left, iron-bound Fur dimers are formed under conditions of iron abundance, and these dimers bind to Fur boxes in their respective target promoters and activate gene transcription. On the right, apo-Fur dimers form under low-iron conditions. These apo-Fur dimers bind to Fur boxes in their target promoters and activate gene transcription. (Right) apo-Fur repression. Under iron depletion conditions, Fur is in its apo form, and apo-Fur binds to the Fur boxes of its target promoters. This binding blocks the binding of RNA polymerase; hence, transcription is repressed. For the sake of simplicity, apo-Fur repression and activation are depicted as being mediated through an apo-Fur dimer, although it is not known whether apo-Fur functions as a monomer or a dimer. Abbreviated lists of organisms that utilize each type of Fur regulation are listed in each panel. An asterisk indicates organisms for which apo-Fur regulation has been suggested but direct interaction has not yet been determined.

References

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