Affiliation:
1. Mikrobiologie/Membranphysiologie, Universität Tübingen, D-72076 Tübingen, Germany
Abstract
ABSTRACT
Replacement of glutamate 176, the only charged amino acid in the third transmembrane helix of ExbB, with alanine (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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
16 articles.
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