caa a22 4500 467895201 CHVBK 20180406152801.0 cr unu---uuuuu 170328e20060901xx s 000 0 eng 10.1007/s11103-006-9015-0 doi (NATIONALLICENCE)springer-10.1007/s11103-006-9015-0 Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana [Elektronische Daten] [Ulrika Schagerlöf, Greer Wilson, Hans Hebert, Salam Al-Karadaghi, Cecilia Hägerhäll] 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. Springer Science+Business Media B.V., 2006 FRO2 nationallicence gp91phox nationallicence Ferric-chelate reductases nationallicence Superoxide generating NADPH oxidases nationallicence Alkaline phosphatase nationallicence Iron transport nationallicence PhoA : Alkaline Phosphatase nationallicence FP : fusion protein nationallicence PCR : polymerase chain reaction nationallicence SDS-PAGE : Sodium dodecyl sulfate-polyacrylamide gel electrophoresis nationallicence Schagerlöf Ulrika Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00, Lund, Sweden aut Wilson Greer Torckpark 25, 6701EE, Wageningen, The Netherlands aut Hebert Hans Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00, Lund, Sweden aut Al-Karadaghi Salam Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00, Lund, Sweden aut Hägerhäll Cecilia Department of Biochemistry, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00, Lund, Sweden aut Plant Molecular Biology Kluwer Academic Publishers 62/1-2(2006-09-01), 215-221 0167-4412 62:1-2<215 2006 62 11103 https://doi.org/10.1007/s11103-006-9015-0 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11103-006-9015-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Schagerlöf Ulrika Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 700 1- Wilson Greer Torckpark 25, 6701EE, Wageningen, The Netherlands aut NATIONALLICENCE 700 1- Hebert Hans Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 700 1- Al-Karadaghi Salam Department of Molecular Biophysics, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 700 1- Hägerhäll Cecilia Department of Biochemistry, Center for Chemistry and Chemical Engineering, Box 124, SE-221 00, Lund, Sweden aut NATIONALLICENCE 773 0- Plant Molecular Biology Kluwer Academic Publishers 62/1-2(2006-09-01), 215-221 0167-4412 62:1-2<215 2006 62 11103 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer