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Review
. 2011 Apr;15(2):335-41.
doi: 10.1016/j.cbpa.2011.01.006. Epub 2011 Feb 1.

Iron-containing transcription factors and their roles as sensors

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Review

Iron-containing transcription factors and their roles as sensors

Angela S Fleischhacker et al. Curr Opin Chem Biol. 2011 Apr.

Abstract

Iron-binding transcription factors are widespread throughout the bacterial world and to date are known to bind several types of cofactors, such as Fe2+, heme, or iron-sulfur clusters. The known chemistry of these cofactors is exploited by transcription factors, including Fur, FNR, and NsrR, to sense molecules such as Fe2+, gases (e.g. oxygen and nitric oxide), or reactive oxygen species. New structural data and information generated by genome-wide analysis studies have provided additional details about the mechanism and function of iron-binding transcription factors that act as sensors.

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Figures

Figure 1
Figure 1
Iron-containing transcription factors. Iron-containing transcription factors bind Fe2+, Fe-S clusters, or heme moieties and can act as sensors of various species, including metals, oxygen, oxidative stress (ox. stress), or nitric oxide (NO). Examples of these sensors are shown here and discussed in this review.

References

    1. Waldron KJ, Robinson NJ. How do bacterial cells ensure that metalloproteins get the correct metal? Nat Rev Microbiol. 2009;7:25–35. - PubMed
    1. Lee JW, Helmann JD. Functional specialization within the Fur family of metalloregulators. Biometals. 2007;20:485–499. - PubMed
    1. Carpenter BM, Whitmire JM, Merrell DS. This is not your mother's repressor: the complex role of Fur in pathogenesis. Infect Immun. 2009;77:2590–2601. - PMC - PubMed
    1. Ahmad R, Brandsdal BO, Michaud-Soret I, Willassen NP. Ferric uptake regulator protein: binding free energy calculations and per-residue free energy decomposition. Proteins: Struct, Funct, and Bioinf. 2009;75:373–386. The authors used computational techniques to determine the site of Fe2+ binding to Fur and the effects of iron ligation. Further, the effects of Fe2+-Fur binding to DNA and the amino acids important for this interaction were investigated.

    1. McHugh JP, Rodriguez-Quinones F, Abdul-Tehrani H, Svistunenko DA, Poole RK, Cooper CE, Andrews SC. Global iron-dependent gene regulation in Escherichia coli: a new mechanism for iron homeostasis. J Biol Chem. 2003;278:29478–29486. - PubMed

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