Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli.
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Chan CS, Howell JM, Workentine ML, Turner RJ
Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli.
Biochem Biophys Res Commun. 2006 Apr 28;343(1):244-51. Epub 2006 Mar 3.
- PubMed ID
- 16540088 [ View in PubMed]
- Abstract
NarJ is a chaperone involved in folding, maturation, and molybdenum cofactor insertion of nitrate reductase A from Escherichia coli. It has also been shown that NarJ exhibits sequence homology to a family of chaperones involved in maturation and cofactor insertion of E. coli redox enzymes that are mediated by twin-arginine translocase (Tat) dependent translocation. In this study, we show that NarJ binds the N-terminal region of NarG through Far Western studies and isothermal titration calorimetry, and the binding event occurs towards a short peptide sequence that contains a homologous twin-arginine motif. Fractionation experiments also show that the interaction of NarJ to the cytoplasmic membrane exhibits Tat-dependence. Upon further investigation through Far Western blots, the interactome of NarJ also exhibits Tat-dependence. Together the data suggest that the Tat system may play a role in the maturation pathway of nitrate reductase A.