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Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana
KTH, School of Technology and Health (STH), Structural Biotechnology.ORCID iD: 0000-0002-3220-9402
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2006 (English)In: Plant Molecular Biology, ISSN 0167-4412, E-ISSN 1573-5028, Vol. 62, no 02-jan, 215-221 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2006. Vol. 62, no 02-jan, 215-221 p.
Keyword [en]
FRO2, gp91phox, ferric-chelate reductases, superoxide generating NADPH oxidases, alkaline phosphatase, iron transport, nadh-quinone oxidoreductase, escherichia-coli, saccharomyces-cerevisiae, iron uptake, subunit, transport, homologs, oxidase, protein
URN: urn:nbn:se:kth:diva-15981ISI: 000240399300016OAI: diva2:334023
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2010-10-04Bibliographically approved

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