کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2187605 | 1096128 | 2008 | 12 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Characterization of a Novel Prokaryotic GDP Dissociation Inhibitor Domain from the G Protein Coupled Membrane Protein FeoB Characterization of a Novel Prokaryotic GDP Dissociation Inhibitor Domain from the G Protein Coupled Membrane Protein FeoB](/preview/png/2187605.png)
The FeoB family of membrane embedded G proteins are involved with high affinity Fe(II) uptake in prokaryotes. Here, we report that FeoB harbors a novel GDP dissociation inhibitor-like domain that specifically stabilizes GDP-binding through an interaction with the switch I region of the G protein. We show that the stabilization of GDP binding is conserved between species despite a high degree of sequence variability in their guanine nucleotide dissociation inhibitor (GDI)-like domains, and demonstrate that the presence of the membrane embedded domain increases GDP-binding affinity roughly 150-fold over the level accomplished by action of the GDI-like domain alone. To our knowledge, this is the first example for a prokaryotic GDI, targeting a bacterial G protein-coupled membrane process. Our findings suggest that Fe(II) uptake in bacteria involves a G protein regulatory pathway reminiscent of signaling mechanisms found in higher-order organisms.
Journal: Journal of Molecular Biology - Volume 375, Issue 4, 25 January 2008, Pages 1086–1097