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Two-component bacterial multidrug transporter, EbrAB: Mutations making each component solely functional

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/14584

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)

Submitter: 菊川 峰志

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