Characterization of a Novel Prokaryotic GDP Dissociation Inhibitor Domain from the G Protein Coupled Membrane Protein FeoB

Edward T. Eng, Amir R. Jalilian, Krasimir A. Spasov, Vinzenz M. Unger*

*Corresponding author for this work

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1086-1097
Number of pages12
JournalJournal of Molecular Biology
Volume375
Issue number4
DOIs
StatePublished - Jan 25 2008

Keywords

  • Fe(II)-uptake
  • GTP-binding protein
  • bacterial proteins
  • guanine nucleotide dissociation inhibitor
  • switch region

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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