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The molecular mechanisms of the bacterial iron sensor IdeR
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 regulat...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10317159/ https://www.ncbi.nlm.nih.gov/pubmed/37140254 http://dx.doi.org/10.1042/BST20221539 |
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author | Marcos-Torres, Francisco Javier Juniar, Linda Griese, Julia J. |
author_facet | Marcos-Torres, Francisco Javier Juniar, Linda Griese, Julia J. |
author_sort | Marcos-Torres, Francisco Javier |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-10317159 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-103171592023-07-04 The molecular mechanisms of the bacterial iron sensor IdeR Marcos-Torres, Francisco Javier Juniar, Linda Griese, Julia J. Biochem Soc Trans Review Articles 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. Portland Press Ltd. 2023-06-28 2023-05-04 /pmc/articles/PMC10317159/ /pubmed/37140254 http://dx.doi.org/10.1042/BST20221539 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . Open access for this article was enabled by the participation of Uppsala University in an all-inclusive Read & Publish agreement with Portland Press and the Biochemical Society under a transformative agreement with Bibsam. |
spellingShingle | Review Articles Marcos-Torres, Francisco Javier Juniar, Linda Griese, Julia J. The molecular mechanisms of the bacterial iron sensor IdeR |
title | The molecular mechanisms of the bacterial iron sensor IdeR |
title_full | The molecular mechanisms of the bacterial iron sensor IdeR |
title_fullStr | The molecular mechanisms of the bacterial iron sensor IdeR |
title_full_unstemmed | The molecular mechanisms of the bacterial iron sensor IdeR |
title_short | The molecular mechanisms of the bacterial iron sensor IdeR |
title_sort | molecular mechanisms of the bacterial iron sensor ider |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10317159/ https://www.ncbi.nlm.nih.gov/pubmed/37140254 http://dx.doi.org/10.1042/BST20221539 |
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