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Journal of Bacteriology, October 2007, p. 7206-7212, Vol. 189, No. 20
0021-9193/07/$08.00+0 doi:10.1128/JB.00871-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Barry L. Taylor, and
Mark S. Johnson*
Division of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, California 92350
Received 5 June 2007/ Accepted 30 July 2007
The Aer receptor guides Escherichia coli to specific oxygen and energy-generating niches. The input sensor in Aer is a flavin adenine dinucleotide-binding PAS domain, which is separated from a HAMP/signaling output domain by two membrane-spanning segments that flank a short (four-amino-acid) periplasmic loop. In this study, we determined the overall membrane organization of Aer by introducing combinations of residues that allowed us to differentiate intradimeric collisions from interdimeric collisions. Collisions between proximal residues in the membrane anchor were exclusively intra- or interdimeric but, with one exception, not both. Cross-linking profiles were consistent, with a rigid rather than flexible periplasmic loop and a tilted TM2 helix that crossed TM2' at residue V197C, near the center of the lipid bilayer. The periplasmic loop formed a stable neighborhood that (i) included a maximum of three Aer dimers, (ii) did not swap neighbors over time, and (iii) appeared to be constrained by interactions in the cytosolic signaling domain.
Published ahead of print on 10 August 2007.
Present address: Department of Biochemistry, University of Missouri-Columbia, Columbia, MO 65211.
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