Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana

Ulrika Schagerlöf, Greer Wilson, Hans Hebert, Salam Al-Karadaghi, Cecilia Hägerhäll

Research output: Contribution to journalArticlepeer-review

31 Citations (SciVal)

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.
Original languageEnglish
Pages (from-to)215-221
JournalPlant Molecular Biology
Volume62
Issue number1-2
DOIs
Publication statusPublished - 2006

Subject classification (UKÄ)

  • Biological Sciences

Keywords

  • gp91phox
  • FRO2
  • ferric-chelate reductases
  • oxidases
  • superoxide generating NADPH
  • iron transport
  • alkaline phosphatase

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