Basis of recognition between the NarJ chaperone and the N‐terminus of the NarG subunit from <i>Escherichia coli</i> nitrate reductase

Zakian, S.; Lafitte, Daniel; Vergnes, Alexandra; Pimentel, Cyril; Sebban‐Kreuzer, Corinne; Toci, René; Claude, Jean‐Baptiste; Guerlesquin, Françoise; Magalon, Axel

doi:10.1111/j.1742-4658.2010.07611.x

Cited by 28 publications

(48 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This subunit uses nitrate as the electron acceptor, reducing it to nitrite [53]. NarJ assists in the insertion of molybdenum cofactor in NarG, which must happen before the interaction between NarGH and NarI [54]. NarK is a transporter that performs nitrate/nitrite exchange [55].…”

Section: Resultsmentioning

confidence: 99%

Comparative genomic analysis between Corynebacterium pseudotuberculosis strains isolated from buffalo

et al. 2017

View full text Add to dashboard Cite

Corynebacterium pseudotuberculosis is a Gram-positive, pleomorphic, facultative intracellular pathogen that causes Oedematous Skin Disease (OSD) in buffalo. To better understand the pathogenic mechanisms of OSD, we performed a comparative genomic analysis of 11 strains of C. pseudotuberculosis isolated from different buffalo found to be infected in Egypt during an outbreak that occurred in 2008. Sixteen previously described pathogenicity islands (PiCp) were present in all of the new buffalo strains, but one of them, PiCp12, had an insertion that contained both a corynephage and a diphtheria toxin gene, both of which may play a role in the adaptation of C. pseudotuberculosis to this new host. Synteny analysis showed variations in the site of insertion of the corynephage during the same outbreak. A gene functional comparison showed the presence of a nitrate reductase operon that included genes involved in molybdenum cofactor biosynthesis, which is necessary for a positive nitrate reductase phenotype and is a possible adaptation for intracellular survival. Genomes from the buffalo strains also had fusions in minor pilin genes in the spaA and spaD gene cluster (spaCX and spaYEF), which could suggest either an adaptation to this particular host, or mutation events in the immediate ancestor before this particular epidemic. A phylogenomic analysis confirmed a clear separation between the Ovis and Equi biovars, but also showed what appears to be a clustering by host species within the Equi strains.

show abstract

Section: Resultsmentioning

confidence: 99%

Comparative genomic analysis between Corynebacterium pseudotuberculosis strains isolated from buffalo

et al. 2017

View full text Add to dashboard Cite

show abstract

“…The NarJ is a chaperone that is involved in folding, maturation, and molybdenum cofactor insertion of nitrate reductase in E. coli [51, 52]. The similarity values found between C. pseudotuberculosis biovar Equi and other sequences of orthologous proteins by BLAST, including the genus Corynebacterium , were slightly lower than those found in other proteins (NarG, NarH, and NarI) that form the three subunits of the enzyme nitrate reductase (Table 2).…”

Section: Resultsmentioning

confidence: 99%

Exploration of Nitrate Reductase Metabolic Pathway inCorynebacterium pseudotuberculosis

Almeida

Sousa

Abreu

et al. 2017

International Journal of Genomics

View full text Add to dashboard Cite

Based on the ability of nitrate reductase synthesis, Corynebacterium pseudotuberculosis is classified into two biovars: Ovis and Equi. Due to the presence of nitrate reductase, the Equi biovar can survive in absence of oxygen. On the other hand, Ovis biovar that does not have nitrate reductase is able to adapt to various ecological niches and can grow on certain carbon sources. Apart from these two biovars, some other strains are also able to carry out the reduction of nitrate. The enzymes that are involved in electron transport chain are also identified by in silico methods. Findings about pathogen metabolism can contribute to the identification of relationship between nitrate reductase and the C. pseudotuberculosis pathogenicity, virulence factors, and discovery of drug targets.

show abstract

“…45 At lower pH (pH 7.0), when the stoichiometry values showed less than one binding site, it was concluded to be due to two forms of the NarJ protein, each with a different protonated state and each with different affinities for NarG. 45,46 At the higher pH 8.0, NarJ bound to NarG with reduced affinity but as a single 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 23 Without a structure of the DmsD-DmsAL complex, it is not possible to specify exactly where changes in entropy are occurring since total entropy of binding is made up of multiple components that may shift during the course of the formation of the complex. 48 The majority of favorable entropy is believed to be due to the release of water from the surface of a binding site;…”

Section: Stoichiometry Of Binding and Hydrodynamic Characterization Omentioning

confidence: 97%

Thermodynamic Characterization of the DmsD Binding Site for the DmsA Twin-Arginine Motif

Winstone

Turner

2015

Biochemistry

View full text Add to dashboard Cite

The system specific chaperone DmsD interacts with the twin-arginine leader peptide of its substrate, DmsA, allowing for proper folding and assembly of the DmsA catalytic subunit of dimethyl sulfoxide reductase prior to translocation by the twin-arginine translocase. DmsD residues important for binding the complete 45-amino acid sequence of the DmsA leader (DmsAL) peptide were previously identified and found to cluster in a pocket of the DmsD structure. In this study, we have utilized isothermal titration calorimetry (ITC) to determine the dissociation constant and thermodynamic parameters of 15 single-substitution DmsD variant proteins and a synthetic DmsAL peptide consisting of 27 amino acids (DmsAL₁₅₋₄₁). The stoichiometry values were determined via ITC, and the multimeric compositions of the DmsD variants in the absence and presence of peptide were characterized via size exclusion chromatography and native polyacrylamide gel electrophoresis. An up to 4-fold change in affinity was observed for DmsD variant proteins relative to that of wild-type DmsD, and variation of the entropic contribution to binding divided the binding site into two clusters: residues with either more or less favorable entropy. Substitution of hydrophobic residues along one helix face (helix 5) or prolines found on adjacent loops caused reduced binding affinity because of the increased entropic cost, which suggests that the twin-arginine motif of the DmsAL peptide binds to a preformed site on DmsD. Most DmsD variants were more than 90% monomeric in solution and bound a single peptide per protein molecule. The DmsD variant with the largest dimer population showed increased affinity and induced the formation of tetramers in the presence of peptide, suggesting that dimeric DmsD or an alternatively folded form of DmsD may play an as yet undefined role in binding.

show abstract

Basis of recognition between the NarJ chaperone and the N‐terminus of the NarG subunit from Escherichia coli nitrate reductase

Cited by 28 publications

References 29 publications

Comparative genomic analysis between Corynebacterium pseudotuberculosis strains isolated from buffalo

Comparative genomic analysis between Corynebacterium pseudotuberculosis strains isolated from buffalo

Exploration of Nitrate Reductase Metabolic Pathway inCorynebacterium pseudotuberculosis

Thermodynamic Characterization of the DmsD Binding Site for the DmsA Twin-Arginine Motif

Contact Info

Product

Resources

About