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Two-component bacterial multidrug transporter, EbrAB: Mutations making each component solely functional
| Title: | Two-component bacterial multidrug transporter, EbrAB: Mutations making each component solely functional |
| Authors: | Kikukawa, Takashi Browse this author →KAKEN DB | | Nara, Toshifumi Browse this author | | Araiso, Tsunehisa Browse this author | | Miyauchi, Seiji Browse this author | | Kamo, Naoki Browse this author |
| Keywords: | EbrAB | | EmrE | | Smr | | Ion-coupled transporter | | Multidrug resistance |
| Issue Date: | May-2006 |
| Publisher: | Elsevier B.V. |
| Journal Title: | Biochimica et Biophysica Acta (BBA) - Biomembranes |
| Volume: | 1758 |
| Issue: | 5 |
| Start Page: | 673 |
| End Page: | 679 |
| Publisher DOI: | 10.1016/j.bbamem.2006.04.004 |
| PMID: | 16750162 |
| Abstract: | EbrAB in Bacillus subtilis belongs to a novel small multidrug resistance (SMR) family of multidrug efflux pumps. EmrE in Escherichia coli, a representative of SMR, functions as a homo-oligomer in the membrane. On the other hand, EbrAB requires a hetero-oligomeric configuration consisting of two polypeptides, EbrA and EbrB. Although both polypeptides have a high sequence similarity, expression of either single polypeptide does not confer the multidrug-resistance. We performed mutation studies on EbrA and B to determine why EbrAB requires the hetero-oligomerization. Mutants of EbrA and B lacking both the hydrophilic loops and the C-terminus regions conferred the multidrug-resistance solely by each protein. This suggests that the hydrophilic loops and the C-terminus regions constrain them to their respective conformations upon the formation of the functional hetero-oligomer. |
| Relation: | http://www.sciencedirect.com/science/journal/00052736 |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/14584 |
| 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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