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IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
The finding that IscR activity is decreased in strain backgrounds in which Fe-S cluster assembly is impaired suggests that this protein may be part of a novel autoregulatory mechanism that senses the Fe-sulfur cluster assembly status of cells. Expand
Iron-sulfur clusters: nature's modular, multipurpose structures.
Iron-sulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occurrence and multiplicity of function. Expand
DNA Binding and Dimerization of the Fe−S-containing FNR Protein from Escherichia coli Are Regulated by Oxygen (*)
Observations suggest that oxygen regulates the activity of wild-type FNR through the lability of the Fe-S cluster to oxygen. Expand
Oxygen sensing by the global regulator, FNR: the role of the iron-sulfur cluster.
According to Mössbauer spectroscopy on purified FNR and cells containing overexpressed FNR, the [4Fe-4S]2+ cluster of FNR is converted by O2 to a [2Fe-2S)2+ in high yield and the ability to observe the Fe-S clusters of F NR in cells containing high levels of FNH should be of value in further unraveling how FNR functions in vivo. Expand
Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae.
It is suggested that NFU1 and ISU1 gene products play a role in iron homeostasis, perhaps in assembly, insertion, and/or repair of mitochondrial Fe-S clusters. Expand
Iron-sulfur proteins: ancient structures, still full of surprises
  • H. Beinert
  • Chemistry, Medicine
  • JBIC Journal of Biological Inorganic Chemistry
  • 1 February 2000
This article is a survey of the properties and functions of Fe-S proteins under the following headings: sulfur and iron; iron-sulfur clusters; evolution of cofactor use; early observations; complexExpand
Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity.
The transcription factor FNR (fumarate nitrate reduction) requires the presence of an iron-sulfur (Fe-S) cluster for its function as a global transcription regulator in Escherichia coli when oxygenExpand
The role of Fe-S proteins in sensing and regulation in bacteria.
Experimental data and bioinformatic predictions suggest that homologs of FNR, IscR and SoxR exist in other bacterial species, highlighting the widespread nature of Fe-S-dependent regulatory networks. Expand
Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding.
The observation that DNA binding is enhanced when the Fe-S center is reduced indicates that the redox state of the Fe -S center affects the DNA-binding activity of this protein and suggests a possible mechanism for regulation of the wild-type protein. Expand