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PNAS 99 (25): 16243-16248

Copyright © 2002 by the National Academy of Sciences.


BIOLOGICAL SCIENCES / MICROBIOLOGY

The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria

Thomas C. Marlovits*, Winfried Haase{dagger}, Christian Herrmann{ddagger}, Stephen G. Aller*, and Vinzenz M. Unger*,§

*Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, P.O. Box 208024, New Haven, CT 06520-8024; {dagger}Department of Structural Biology, Max Planck Institute for Biophysics, Heinrich-Hoffmann-Strasse 7, D-60528 Frankfurt, Germany; and {ddagger}Department of Structural Biology, Max Planck Institute for Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany

Received for publication June 5, 2002.

Abstract: G proteins are critical for the regulation of membrane protein function and signal transduction. Nevertheless, coupling between G proteins and membrane proteins with multiple membrane-spanning domains has so far been observed only in higher organisms. Here we show that the polytopic membrane protein FeoB, which is essential for Fe(II) uptake in bacteria, contains a guanine-nucleotide-specific nucleotide binding site. We identify the G4-motif, NXXD, responsible for guanine nucleotide specificity, and show that GTP hydrolysis occurs very slowly. In contrast to typical G proteins, the association and dissociation of GDP were found to be faster than for GTP, suggesting that in the absence of additional factors, FeoB's G protein domain may exist mostly in the GTP-bound form. Furthermore, the binding of GTP is required for efficient Fe(II) uptake through the FeoB-dependent system. Notably, even in bacteria, this covalent linkage between a G protein and a polytopic membrane protein appears, to our knowledge, to be unique. These findings raise the intriguing question whether FeoB represents a primordial archetype of G protein-regulated membrane proteins.


§ To whom correspondence should be addressed at: Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, P.O. Box 208024, 333 Cedar Street, New Haven, CT 06520-8024. E-mail: vinzenz.unger{at}yale.edu.

Edited by Jonathan Beckwith, Harvard Medical School, Boston, MA, and approved September 30, 2002

This paper was submitted directly (Track II) to the PNAS office.


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