Heme binds to and inhibits the DNA‐binding activity of the global regulator FurA from <i>Anabaena</i> sp. PCC 7120

Hernández, José Ángel; Peleato, M. Luisa; Fillat, Marı́a F.; Bes, M. Teresa

doi:10.1016/j.febslet.2004.09.060

Cited by 34 publications

(48 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Fur-DNA interactions have also been influenced by the presence of heme (Hernandez et al 2004b). The involvement of heme in regulating important bacterial metabolic pathways such as respiration and energy transfer is already well documented (Smith et al 1996).…”

Section: Fur-dna Interactionmentioning

confidence: 97%

“…Differential spectroscopy-based analyses have identified the presence of a Fur-heme complex in the cyanobacterium Anabaena sp. PCC 7120 (Hernandez et al 2004b). Heme binds and inhibits the DNA binding ability of the Fur protein in vitro in a concentration dependent manner, which represses the expression of Fur-regulated genes (Hernandez et al 2004b).…”

Section: Fur-dna Interactionmentioning

confidence: 99%

“…The affinity, stability and quality of Fur-DNA interaction in cyanobacteria can be influenced by several factors, such as the architecture of Fur boxes, the presence of divalent metal ions, the redox status of cysteine and histidine residues within the Fur protein, ionic interactions (Hernandez et al 2002(Hernandez et al , 2006b) and the involvement of effectors like heme (Hernandez et al 2004b;Pellicer et al 2012). It was previously considered that the A and T bases at position 5 and 6 of the consensus hexamer played a major role in the Fur-DNA interaction (Escolar et al 1998).…”

Section: Fur-dna Interactionmentioning

confidence: 99%

See 2 more Smart Citations

Ferric Uptake Regulator (FUR) protein: properties and implications in cyanobacteria

et al. 2015

View full text Add to dashboard Cite

The Ferric uptake regulator (Fur) protein is a global iron regulator found in most prokaryotes. Although the Fur protein is involved in a variety of metabolic pathways, it is specifically known for the regulation of several iron responsive genes. It binds to the highly conserved sequences located in the upstream promoter region known as iron boxes, using ferrous ion as a co-repressor. Apart from that, the Fur protein is also directly/indirectly involved in a variety of other crucial physiological pathways. Hence, understanding the mechanism of action and the mechanistic pathways of iron regulation by Fur is necessary and important. The basic understanding of the functioning and properties of Fur protein along with its role, interaction and regulation at various levels in cyanobacteria has been discussed in detail.

show abstract

Section: Fur-dna Interactionmentioning

confidence: 97%

Section: Fur-dna Interactionmentioning

confidence: 99%

Section: Fur-dna Interactionmentioning

confidence: 99%

See 1 more Smart Citation

Ferric Uptake Regulator (FUR) protein: properties and implications in cyanobacteria

et al. 2015

View full text Add to dashboard Cite

show abstract

“…FurA is a multifaceted protein that controls iron homeostasis and modulates an extensive regulon involved in a variety of cell functions (13,14,15). It also fulfills the features of a heme sensor protein whose interaction with this cofactor negatively affects its DNA binding ability in vitro (23,41).…”

Section: Innovationmentioning

confidence: 99%

Cysteine Mutational Studies Provide Insight into a Thiol-Based Redox Switch Mechanism of Metal and DNA Binding in FurA fromAnabaenasp. PCC 7120

Botello-Morte

Pellicer

Sein‐Echaluce

et al. 2016

Antioxidants & Redox Signaling

View full text Add to dashboard Cite

Aims: The ferric uptake regulator (Fur) is the main transcriptional regulator of genes involved in iron homeostasis in most prokaryotes. FurA from Anabaena sp. PCC 7120 contains five cysteine residues, four of them arranged in two redox-active CXXC motifs. The protein needs not only metal but also reducing conditions to remain fully active in vitro. Through a mutational study of the cysteine residues present in FurA, we have investigated their involvement in metal and DNA binding. , suggesting that the environments of these cysteines are mutually interdependent. Innovation: We propose that C 101 is part of a thiol/disulfide redox switch that determines FurA ability to bind the metal corepressor. Conclusion: This mechanism supports a novel feature of a Fur protein that emerges as a regulator, which connects the response to changes in the intracellular redox state and iron management in cyanobacteria. Antioxid. Redox Signal. 24, 173-185.

show abstract

“…The best-known system of iron homeostasis in bacteria is mediated by the Fur (ferric uptake regulator) transcriptional regulator, which has been extensively studied in various taxonomic groups including c-and b-proteobacteria, bacilli, and cyanobacteria [7][8][9][10][11][12][13][14][15][16]. When Fur interacts with ferrous iron in Fe-replete conditions, it binds avidly to conserved sequences, known as FUR-boxes, and represses the initiation of transcription of its target genes.…”

Section: Introductionmentioning

confidence: 99%

Computational reconstruction of iron- and manganese-responsive transcriptional networks in alpha-proteobacteria

Rodionov¹,

Gelfand²,

Todd³

et al. 2005

PLoS Comp Biol

View full text Add to dashboard Cite

We used comparative genomics to investigate the distribution of conserved DNA-binding motifs in the regulatory regions of genes involved in iron and manganese homeostasis in alpha-proteobacteria. Combined with other computational approaches, this allowed us to reconstruct the metal regulatory network in more than three dozen species with available genome sequences. We identified several classes of cis-acting regulatory DNA motifs (Irr-boxes or ICEs, RirA-boxes, Iron-Rhodo-boxes, Fur-alpha-boxes, Mur-box or MRS, MntR-box, and IscR-boxes) in regulatory regions of various genes involved in iron and manganese uptake, Fe-S and heme biosynthesis, iron storage, and usage. Despite the different nature of the iron regulons in selected lineages of alpha-proteobacteria, the overall regulatory network is consistent with, and confirmed by, many experimental observations. This study expands the range of genes involved in iron homeostasis and demonstrates considerable interconnection between iron-responsive regulatory systems. The detailed comparative and phylogenetic analyses of the regulatory systems allowed us to propose a theory about the possible evolution of Fe and Mn regulons in alpha-proteobacteria. The main evolutionary event likely occurred in the common ancestor of the Rhizobiales and Rhodobacterales, where the Fur protein switched to regulating manganese transporters (and hence Fur had become Mur). In these lineages, the role of global iron homeostasis was taken by RirA and Irr, two transcriptional regulators that act by sensing the physiological consequence of the metal availability rather than its concentration per se, and thus provide for more flexible regulation.

show abstract

Heme binds to and inhibits the DNA‐binding activity of the global regulator FurA from Anabaena sp. PCC 7120

Cited by 34 publications

References 41 publications

Ferric Uptake Regulator (FUR) protein: properties and implications in cyanobacteria

Ferric Uptake Regulator (FUR) protein: properties and implications in cyanobacteria

Cysteine Mutational Studies Provide Insight into a Thiol-Based Redox Switch Mechanism of Metal and DNA Binding in FurA fromAnabaenasp. PCC 7120

Computational reconstruction of iron- and manganese-responsive transcriptional networks in alpha-proteobacteria

Contact Info

Product

Resources

About