کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1941032 | 1050793 | 2006 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli Twin-arginine translocase may have a role in the chaperone function of NarJ from Escherichia coli](/preview/png/1941032.png)
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.
Journal: Biochemical and Biophysical Research Communications - Volume 343, Issue 1, 28 April 2006, Pages 244–251