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Journal of Bacteriology, July 2004, p. 4402-4406, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4402-4406.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Point Mutations in Transmembrane Helices 2 and 3 of ExbB and TolQ Affect Their Activities in Escherichia coli K-12

Volkmar Braun* and Christina Herrmann

Mikrobiologie/Membranphysiologie, Universität Tübingen, D-72076 Tübingen, Germany

Received 6 February 2004/ Accepted 1 April 2004

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.

* Corresponding author. Mailing address: Mikrobiologie/Membranphysiologie, Universität Tübingen, Auf der Morgenstelle 28, D-72076 Tübingen, Germany. Phone: (49) 7071 2972096. Fax: (49) 7071 29 5843. E-mail: volkmar.braun{at}mikrobio.uni-tuebingen.de.

Journal of Bacteriology, July 2004, p. 4402-4406, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4402-4406.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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