Crystal structure of <i>Campylobacter jejuni</i> peroxide regulator

Sarvan, Sabina; Charih, François; Butcher, James; Brunzelle, J.S.; Stintzi, Alain; Couture, Jean

doi:10.1002/1873-3468.13120

Cited by 7 publications

(2 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several structural studies have elucidated how PerR responds to peroxide stresses and undergoes structural changes to induce peroxide stress responses [58][59][60][61][62][63][64] (Table 1). In B. subtilis PerR, four cysteine residues (Cys96, Cys99, Cys136 and Cys139) cluster to form a Zn2+-binding site, while three histidine and two aspartate residues (His3Asp2; His37, Asp85, His91, His93 and Asp104) coordinate the regulatory metal ion Fe2+ or Mn2+ [62,63].…”

Section: Sensing By Fe-catalyzed Histidine Oxidation: Perrmentioning

confidence: 99%

How Bacterial Redox Sensors Transmit Redox Signals via Structural Changes

Lee

2021

Antioxidants

View full text Add to dashboard Cite

Bacteria, like humans, face diverse kinds of stress during life. Oxidative stress, which is produced by cellular metabolism and environmental factors, can significantly damage cellular macromolecules, ultimately negatively affecting the normal growth of the cell. Therefore, bacteria have evolved a number of protective strategies to defend themselves and respond to imposed stress by changing the expression pattern of genes whose products are required to convert harmful oxidants into harmless products. Structural biology combined with biochemical studies has revealed the mechanisms by which various bacterial redox sensor proteins recognize the cellular redox state and transform chemical information into structural signals to regulate downstream signaling pathways.

show abstract

Section: Sensing By Fe-catalyzed Histidine Oxidation: Perrmentioning

confidence: 99%

How Bacterial Redox Sensors Transmit Redox Signals via Structural Changes

Lee

2021

Antioxidants

View full text Add to dashboard Cite

show abstract

“…Members of the Fur superfamily are composed of two regions: an N-terminal DNA-binding domain, containing a winged-helix motif, and a C-terminal dimerization domain, connected by a hinge loop (Lucarelli et al, 2007; Sheikh and Taylor, 2009; Dian et al, 2011; Butcher et al, 2012; Sarvan et al, 2018c). Fur from Pseudomonas aeruginosa possesses two zinc binding sites.…”

Section: Introductionmentioning

confidence: 99%

Porphyromonas gingivalis PgFur Is a Member of a Novel Fur Subfamily With Non-canonical Function

Śmiga

Bielecki

Olczak

et al. 2019

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Porphyromonas gingivalis , a keystone pathogen of chronic periodontitis, uses ferric uptake regulator homolog (PgFur) to regulate production of virulence factors. This study aimed to characterize PgFur protein in regard to its structure-function relationship. We experimentally identified the 5′ mRNA sequence encoding the 171-amino-acid-long PgFur protein in the A7436 strain and examined this PgFur version as a full-length protein. PgFur protein did not bind to the canonical Escherichia coli Fur box, but the wild-type phenotype of the mutant Δ pgfur strain was restored partially when expression of the ecfur gene was induced from the native pgfur promoter. The full-length PgFur protein contained one zinc atom per protein monomer, but did not bind iron, manganese, or heme. Single cysteine substitutions of CXXC motifs resulted in phenotypes similar to the mutant Δ pgfur strain. The modified proteins were produced in E. coli at significantly lower levels, were highly unstable, and did not bind zinc. The pgfur gene was expressed at the highest levels in bacteria cultured for 24 h in the absence of iron and heme or at higher levels in bacteria cultured for 10 h in the presence of protoporphyrin IX source. No influence of high availability of Fe 2+ , Zn 2+ , or Mn 2+ on pgfur gene expression was observed. Two chromosomal mutant strains producing protein lacking 4 ( pgfur Δ 4aa ) or 13 ( pgfur Δ 13aa ) C-terminal amino acid residues were examined in regard to importance of the C-terminal lysine-rich region. The pgfur Δ 13aa strain showed a phenotype typical for the mutant Δ pgfur strain, but both the wild-type PgFur protein and its truncated version bound zinc with similar ability. The Δ pgfur mutant strain produced higher amounts of HmuY protein compared with the wild-type strain, suggesting compromised regulation of its expression. Potential PgFur ligands, Fe 2+ , Mn 2+ , Zn 2+ , PPIX, or serum components, did not influence HmuY production in the Δ pgfur mutant strain. The mutant pgfur Δ 4aa and pgfur Δ 13aa strains exhibited affected HmuY protein production. PgFur, regardless of the presence of the C-terminal lysine-rich region, bound to the hmu operon promoter. Our data suggest that cooperation of PgFur with partners/cofactors and/or protein/DNA modifications would be required to accomplish its role played in an in vivo multilayer regulatory net...

show abstract

Variation on a theme: investigating the structural repertoires used by ferric uptake regulators to control gene expression

et al. 2018

View full text Add to dashboard Cite

In every living organism, the control of metal homoeostasis is a tightly regulated process coordinated by several intertwined biological pathways. In many bacteria, the ferric uptake regulator (Fur) family of transcriptional factors (TFs) are key factors in controlling the expression of genes involved in metal homeostasis and can also regulate the expression of genes involved in responses to oxidative stresses. Since the crystallization of Escherichia coli Fur DNA binding domain, the crystal structure of several metalloregulators have been reported. While the Fur family of proteins adopt similar structures, each contains unique structural features relating to their specific biological functions. Moreover, recent groundbreaking studies have provided additional insights into the mechanisms underlying the binding of DNA by these metalloregulators. In this review, we present a comprehensive overview of the crystal structure of Fur family metalloregulators with a specific focus on the new structures of these TFs bound to DNA.

show abstract

Crystal structure of Campylobacter jejuni peroxide regulator

Cited by 7 publications

References 37 publications

How Bacterial Redox Sensors Transmit Redox Signals via Structural Changes

How Bacterial Redox Sensors Transmit Redox Signals via Structural Changes

Porphyromonas gingivalis PgFur Is a Member of a Novel Fur Subfamily With Non-canonical Function

Variation on a theme: investigating the structural repertoires used by ferric uptake regulators to control gene expression

Contact Info

Product

Resources

About