Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana |
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Authors: | Ulrika Schagerlöf Greer Wilson Hans Hebert Salam Al-Karadaghi Cecilia Hägerhäll |
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Affiliation: | (1) Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00 Lund, Sweden;(2) Torckpark 25, Wageningen , 6701EE, The Netherlands;(3) Department of Biosciences at Novum, Center for Structural Biochemistry, Karolinska Institutet, SE-141 57 Huddinge, Sweden;(4) Department of Biochemistry, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00 Lund, Sweden |
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Abstract: | Iron uptake in Arabidopsis thaliana is mediated by ferric chelate reductase FRO2, a transmembrane protein belonging to the flavocytochrome b family. There is no high resolution structural information available for any member of this family. We have determined the transmembrane topology of FRO2 experimentally using the alkaline phosphatase fusion method. The resulting topology is different from that obtained by theoretical predictions and contains 8 transmembrane helices, 4 of which build up the highly conserved core of the protein. This core is present in the entire flavocytochrome b family. The large water soluble domain of FRO2, which contains NADPH, FAD and oxidoreductase sequence motifs, was located on the inside of the membrane.Electronic Supplementary Material Supplementary material is available to authorised users in the online version of this article at This work was supported by grants from the Swedish Research Council (VR) to S. Al-Karadaghi and Hans Hebert. |
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Keywords: | FRO2 gp91phox Ferric-chelate reductases Superoxide generating NADPH oxidases Alkaline phosphatase Iron transport |
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