PMID:20236317
| Citation |
Zakian, S, Lafitte, D, Vergnes, A, Pimentel, C, Sebban-Kreuzer, C, Toci, R, Claude, JB, Guerlesquin, F and Magalon, A (2010) Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase. FEBS J. 277:1886-95 |
|---|---|
| Abstract |
A novel class of molecular chaperones co-ordinates the assembly and targeting of complex metalloproteins by binding to an amino-terminal peptide of the cognate substrate. We have previously shown that the NarJ chaperone interacts with the N-terminus of the NarG subunit coming from the nitrate reductase complex, NarGHI. In the present study, NMR structural analysis revealed that the NarG(1-15) peptide adopts an alpha-helical conformation in solution. Moreover, NarJ recognizes and binds the helical NarG(1-15) peptide mostly via hydrophobic interactions as deduced from isothermal titration calorimetry analysis. NMR and differential scanning calorimetry analysis revealed a modification of NarJ conformation during complex formation with the NarG(1-15) peptide. Isothermal titration calorimetry and BIAcore experiments support a model whereby the protonated state of the chaperone controls the time dependence of peptide interaction. |
| Links |
PubMed Online version:10.1111/j.1742-4658.2010.07611.x |
| Keywords |
Binding Sites/genetics; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Nitrate Reductase/chemistry; Nitrate Reductase/genetics; Nitrate Reductase/metabolism; Protein Binding/genetics; Protein Conformation; Protein Structure, Secondary; Static Electricity; Thermodynamics |
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