Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12

被引:14
作者
Braun, V [1 ]
Herrmann, C [1 ]
机构
[1] Univ Tubingen, D-72076 Tubingen, Germany
关键词
D O I
10.1128/JB.186.13.4402-4406.2004
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Replacement of glutamate 176, the only charged amino acid in the third transmembrane helix of ExbB, with allanine (E176A) abolished ExbB activity in all determined ExbB-dependent functions of Escherichia coli. Combination of the mutations T148A in the second transmembrane helix and T181A in the third transmembrane helix, proposed to form part of a proton pathway through ExbB, also resulted in inactive ExbB. E176 and T148 are strictly conserved in ExbB and TolQ proteins, and T181 is almost strictly conserved in ExbB, TolQ, and MotA.
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页码:4402 / 4406
页数:5
相关论文
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