caa a22 4500 397494270 CHVBK 20180308164517.0 cr unu---uuuuu 161202e199507 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a124884 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a124884 Iron-Regulated Expression and Membrane Localization of the MagA Protein in Magnetospirillum sp. Strain AMB-1 [Elektronische Daten] [Chikashi Nakamura, Tomoko Kikuchi, J. Grant Burgess, Tadashi Matsunaga] The magA gene from Magnetospirillum sp. strain AMB-1 is required for the synthesis of bacterial magnetic particles (BMPs). This gene has been cloned, sequenced and found to encode a protein which is homologous to the Escherichia coli potassium efflux membrane-binding protein, KefC. By using the firefly luciferase gene (luc) cloned downstream of the magA promoter, the effect of iron on regulation of magA expression was investigated, and transcription of magA was found to be enhanced by low concentrations of iron. Intracellular localization of the MagA protein was studied using magA-luc fusion proteins. The luc gene was cloned downstream of the magA hydrophilic C-terminal domain. Detection of luciferase activity in the cytoplasm, cell membrane, and magnetic particle membrane subcellular fractions confirmed that the MagA fusion protein was localized in the cell membrane. The fusion protein was also detected on the surface of the lipid bilayer covering the magnetic particles. These results suggest that MagA is a membrane-bound protein, the expression of which is enhanced at low iron concentrations. © by the Journal of Biochemistry Regular Papers nationallicence biomineralization nationallicence gene fusion nationallicence magnetic particle nationallicence Magnetospirillum nationallicence protein localization nationallicence Nakamura Chikashi Department of Biotechnology, Tokyo University of Agriculture and Technology Koganei, Tokyo 184 aut Kikuchi Tomoko Department of Biotechnology, Tokyo University of Agriculture and Technology Koganei, Tokyo 184 aut Burgess J. Grant Department of Biological Sciences, Heriot-Watt University, Riccarton Edinburgh EH14 4AS, UK aut Matsunaga Tadashi Department of Biotechnology, Tokyo University of Agriculture and Technology Koganei, Tokyo 184 aut The Journal of Biochemistry Oxford University Press 118/1(1995-07), 23-27 0021-924X 118:1<23 1995 118 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a124884 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a124884 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Nakamura Chikashi Department of Biotechnology, Tokyo University of Agriculture and Technology Koganei, Tokyo 184 aut NATIONALLICENCE 700 1- Kikuchi Tomoko Department of Biotechnology, Tokyo University of Agriculture and Technology Koganei, Tokyo 184 aut NATIONALLICENCE 700 1- Burgess J. Grant Department of Biological Sciences, Heriot-Watt University, Riccarton Edinburgh EH14 4AS, UK aut NATIONALLICENCE 700 1- Matsunaga Tadashi Department of Biotechnology, Tokyo University of Agriculture and Technology Koganei, Tokyo 184 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 118/1(1995-07), 23-27 0021-924X 118:1<23 1995 118 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford