Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase.
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Zakian S, Lafitte D, Vergnes A, Pimentel C, Sebban-Kreuzer C, Toci R, Claude JB, Guerlesquin F, Magalon A
Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase.
FEBS J. 2010 Apr;277(8):1886-95. doi: 10.1111/j.1742-4658.2010.07611.x. Epub 2010 Mar 2.
- PubMed ID
- 20236317 [ View in PubMed]
- 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.