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Anti-parallel membrane topology of two components of EbrAB, a multidrug transporter.
| Title: | Anti-parallel membrane topology of two components of EbrAB, a multidrug transporter. |
| Authors: | Kikukawa, Takashi Browse this author →KAKEN DB | | Miyauchi, Seiji Browse this author | | Araiso, Tsunehisa Browse this author | | Kamo, Naoki Browse this author | | Nara, Toshifumi Browse this author |
| Keywords: | Efflux transporter | | EmrE | | Small multidrug resistance (SMR) | | Dual topology configuration | | Fluorescein-5-maleimide (NEM-fluorescein) | | Ethidium efflux |
| Issue Date: | 13-Jul-2007 |
| Publisher: | Elsevier Inc. |
| Journal Title: | Biochemical and Biophysical Research Communications |
| Volume: | 358 |
| Issue: | 4 |
| Start Page: | 1071 |
| End Page: | 1075 |
| Publisher DOI: | 10.1016/j.bbrc.2007.05.032 |
| PMID: | 17517373 |
| Abstract: | EbrAB is a multidrug-resistance transporter in Bacillus subtilis that belongs to the small multidrug resistance, and requires two polypeptides of both EbrA and EbrB, implying that it functions in the hetero-dimeric state. In this study, we investigated the transmembrane topologies of EbrA and EbrB. Various single-cysteine mutants were expressed in Escherichia coli cells, and the efflux activity was measured. Only mutants having a high activity were used for the topology experiments. The reactivity of a membrane impermeable NEM-fluorescein against the single cysteine of these fully functional mutants was examined when this reactive fluorophore was applied either from the outside or both sides of the cell membrane or in the denatured state. The results clearly showed that EbrA and EbrB have the opposite orientation within the membrane or an anti-parallel configuration. |
| Relation: | http://www.sciencedirect.com/science/journal/0006291X |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/28010 |
| Appears in Collections: | 創成研究機構 (Creative Research Institution) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 菊川 峰志
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