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  • Marcos-Torres, Francisco JavierUppsala universitet,Strukturbiologi,Department of Biotechnology and Environmental Protection, Estación Experimental del Zaidín-CSIC, 18011 Granada, Spain (author)

The molecular mechanisms of the bacterial iron sensor IdeR

  • Article/chapterEnglish2023

Publisher, publication year, extent ...

  • 2023
  • Portland Press,2023
  • electronicrdacarrier

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  • LIBRIS-ID:oai:DiVA.org:uu-501327
  • https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-501327URI
  • https://doi.org/10.1042/bst20221539DOI

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  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:for swepub-publicationtype

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  • Life came to depend on iron as a cofactor for many essential enzymatic reactions. However, once the atmosphere was oxygenated, iron became both scarce and toxic. Therefore, complex mechanisms have evolved to scavenge iron from an environment in which it is poorly bioavailable, and to tightly regulate intracellular iron contents. In bacteria, this is typically accomplished with the help of one key regulator, an iron-sensing transcription factor. While Gram-negative bacteria and Gram-positive species with low guanine-cytosine (GC) content generally use Fur (ferric uptake regulator) proteins to regulate iron homeostasis, Gram-positive species with high GC content use the functional homolog IdeR (iron-dependent regulator). IdeR controls the expression of iron acquisition and storage genes, repressing the former, and activating the latter in an iron-dependent manner. In bacterial pathogens such as Corynebacterium diphtheriae and Mycobacterium tuberculosis, IdeR is also involved in virulence, whereas in non-pathogenic species such as Streptomyces, it regulates secondary metabolism as well. Although in recent years the focus of research on IdeR has shifted towards drug development, there is much left to learn about the molecular mechanisms of IdeR. Here, we summarize our current understanding of how this important bacterial transcriptional regulator represses and activates transcription, how it is allosterically activated by iron binding, and how it recognizes its DNA target sites, highlighting the open questions that remain to be addressed.

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  • Juniar, LindaUppsala universitet,Strukturbiologi(Swepub:uu)linju896 (author)
  • Griese, Julia J.,Docent,1982-Uppsala universitet,Strukturbiologi(Swepub:uu)julgr393 (author)
  • Uppsala universitetStrukturbiologi (creator_code:org_t)

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  • In:Biochemical Society Transactions: Portland Press0300-51271470-8752

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