Ferric Uptake Regulator
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2022 ◽  
pp. 179-196
Author(s):  
Violeta C. Sein-Echaluce ◽  
José Miguel Mulet ◽  
María V. Barja ◽  
M. Luisa Peleato ◽  
María F. Fillat

Microbiology ◽  
2021 ◽  
Vol 167 (12) ◽  
Author(s):  
Takeshi Shimizu ◽  
Manami Onuki ◽  
Shin Suzuki ◽  
Shinichiro Hirai ◽  
Eiji Yokoyama ◽  
...  

Enterohaemorrhagic Escherichia coli (EHEC) produces Shiga toxin 1 (Stx1) and Shiga toxin 2 (Stx2). Although stx1 and stx2 were found within the late operons of the Stx-encoding phages (Stx-phages), stx1 could mainly be transcribed from the stx1 promoter (P Stx1), which represents the functional operator-binding site (Fur box) for the transcriptional regulator Fur (ferric uptake regulator), upstream of stx1. In this study, we found that the production of Stx1 by EHEC was affected by oxygen concentration. Increased Stx1 production in the presence of oxygen is dependent on Fur, which is an Fe2+-responsive transcription factor. The intracellular Fe2+ pool was lower under microaerobic conditions than under anaerobic conditions, suggesting that lower Fe2+ availability drove the formation of less Fe2+-Fur, less DNA binding to the P Stx1 region, and an increase in Stx1 production.


2021 ◽  
Vol 701 ◽  
pp. 108770
Author(s):  
Emma Sevilla ◽  
M. Teresa Bes ◽  
M. Luisa Peleato ◽  
María F. Fillat

2020 ◽  
Vol 11 ◽  
Author(s):  
Lulu Liu ◽  
Xue Feng ◽  
Wei Wang ◽  
Yining Chen ◽  
Zhe Chen ◽  
...  

Ferric uptake regulator (Fur) is a transcriptional regulator playing a central role in iron homeostasis of many bacteria, and Fur inactivation commonly results in pleiotropic phenotypes. In Shewanella oneidensis, a representative of dissimilatory metal-reducing γ-proteobacteria capable of respiring a variety of chemicals as electron acceptors (EAs), Fur loss substantially impairs respiration. However, to date the mechanism underlying the physiological phenomenon remains obscure. This investigation reveals that Fur loss compromises activity of iron proteins requiring biosynthetic processes for their iron cofactors, heme in particular. We then show that S. oneidensis Fur is critical for maintaining heme homeostasis by affecting both its biosynthesis and decomposition of the molecule. Intriguingly, the abundance of iron-containing proteins controlled by H2O2-responding regulator OxyR increases in the fur mutant because the Fur loss activates OxyR. By comparing suppression of membrane-impermeable, membrane-permeable, and intracellular-only iron chelators on heme deficiency and elevated H2O2 resistance, our data suggest that the elevation of the free iron content by the Fur loss is likely to be the predominant factor for the Fur physiology. Overall, these results provide circumstantial evidence that Fur inactivation disturbs bacterial iron homeostasis by altering transcription of its regulon members, through which many physiological processes, such as respiration and oxidative stress response, are transformed.


2020 ◽  
Vol 295 (46) ◽  
pp. 15464-15465
Author(s):  
Roland Lill

For decades, the bacterial ferric uptake regulator (Fur) has been thought to respond to ferrous iron to transcriptionally regulate genes required for balancing iron uptake, storage, and utilization. Because iron binding to Fur has never been confirmed in vivo, the physiological iron-sensing mechanism remains an open question. Fontenot et al. now show that Fur purified from Escherichia coli binds an all-Cys-coordinated [2Fe-2S] cluster. This finding opens the exciting possibility that Fur may join numerous well-studied bacterial, fungal, and mammalian proteins that use FeS clusters for cellular iron regulation.


2020 ◽  
Vol 295 (46) ◽  
pp. 15454-15463 ◽  
Author(s):  
Chelsey R. Fontenot ◽  
Homyra Tasnim ◽  
Kathryn A. Valdes ◽  
Codrina V. Popescu ◽  
Huangen Ding

The ferric uptake regulator (Fur) is a global transcription factor that regulates intracellular iron homeostasis in bacteria. The current hypothesis states that when the intracellular “free” iron concentration is elevated, Fur binds ferrous iron, and the iron-bound Fur represses the genes encoding for iron uptake systems and stimulates the genes encoding for iron storage proteins. However, the “iron-bound” Fur has never been isolated from any bacteria. Here we report that the Escherichia coli Fur has a bright red color when expressed in E. coli mutant cells containing an elevated intracellular free iron content because of deletion of the iron–sulfur cluster assembly proteins IscA and SufA. The acid-labile iron and sulfide content analyses in conjunction with the EPR and Mössbauer spectroscopy measurements and the site-directed mutagenesis studies show that the red Fur protein binds a [2Fe-2S] cluster via conserved cysteine residues. The occupancy of the [2Fe-2S] cluster in Fur protein is ∼31% in the E. coli iscA/sufA mutant cells and is decreased to ∼4% in WT E. coli cells. Depletion of the intracellular free iron content using the membrane-permeable iron chelator 2,2´-dipyridyl effectively removes the [2Fe-2S] cluster from Fur in E. coli cells, suggesting that Fur senses the intracellular free iron content via reversible binding of a [2Fe-2S] cluster. The binding of the [2Fe-2S] cluster in Fur appears to be highly conserved, because the Fur homolog from Hemophilus influenzae expressed in E. coli cells also reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis.


2020 ◽  
Vol 117 (38) ◽  
pp. 23565-23570
Author(s):  
Alexander Mironov ◽  
Tatyana Seregina ◽  
Konstantin Shatalin ◽  
Maxim Nagornykh ◽  
Rustem Shakulov ◽  
...  

l-cysteine is the source of all bacterial sulfurous biomolecules. However, the cytoplasmic level ofl-cysteine must be tightly regulated due to its propensity to reduce iron and drive damaging Fenton chemistry. It has been proposed that inEscherichia colithe component of cytochromebd-I terminal oxidase, the CydDC complex, shuttles excessivel-cysteine from the cytoplasm to the periplasm, thereby maintaining redox homeostasis. Here, we provide evidence for an alternative function of CydDC by demonstrating that thecydDphenotype, unlike that of the bona fidel-cysteine exportereamA, parallels that of thel-cystine importertcyP.Chromosomal induction ofeamA, but not ofcydDC, from a strong pLtetO-1 promoter (Ptet) leads to the increased level of extracellularl-cysteine, whereas induction ofcydDCortcyPcauses the accumulation of cytoplasmicl-cysteine. Congruently, inactivation ofcydDrenders cells resistant to hydrogen peroxide and to aminoglycoside antibiotics. In contrast, induction ofcydDCsensitizes cells to oxidative stress and aminoglycosides, which can be suppressed byeamAoverexpression. Furthermore, inactivation of the ferric uptake regulator (fur)in Ptet-cydDCor Ptet-tcyPcells results in dramatic loss of survival, whereas catalase (katG) overexpression suppresses the hypersensitivity of both strains to H2O2. These results establish CydDC as a reducer of cytoplasmic cystine, as opposed to anl-cysteine exporter, and further elucidate a link between oxidative stress, antibiotic resistance, and sulfur metabolism.


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