Two-component bacterial multidrug transporter, EbrAB: Mutations making each component solely functional
Two-component bacterial multidrug transporter, EbrAB: Mutations making each component solely functional
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DOI：
10.1016/j.bbamem.2006.04.004
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发表时间：
2006-05-01
影响因子：
3.4
通讯作者：
Kamo, Naoki
中科院分区：
文献类型：
--
作者：
Kikukawa, Takashi;Nara, Toshifumi;Kamo, Naoki
枯草芽孢杆菌中的 EbrAB 属于新型小型多药耐药性 (SMR) 多药外排泵家族。大肠杆菌中的 EmrE 是 SMR 的代表，在膜中充当同源寡聚物。另一方面，EbrAB需要由两种多肽EbrA和EbrB组成的异源寡聚构型。尽管两种多肽具有高度的序列相似性，但任一单一多肽的表达均不赋予多重耐药性。我们对 EbrA 和 B 进行了突变研究，以确定为什么 EbrAB 需要异源寡聚化。缺乏亲水环和C末端区域的EbrA和B突变体仅通过每种蛋白质赋予多重耐药性。这表明亲水环和 C 末端区域在形成功能性异源低聚物时将它们限制为各自的构象。 (c) 2006 Elsevier B.V. 保留所有权利。
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 multi drug-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 multi drug-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. (c) 2006 Elsevier B.V. All rights reserved.