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Science 15 January 1988: Vol. 239. no. 4837, pp. 276 - 278 DOI: 10.1126/science.2447650
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Articles
Science, Vol 239, Issue 4837, 276-278
Copyright © 1988 by American Association for the Advancement of Science
Bacterial motility: membrane topology of the Escherichia coli MotB protein
SY Chun
and
JS Parkinson
Biology Department, University of Utah, Salt Lake City 84112.
The MotB protein of Escherichia coli is an essential component of the force generators that couple proton movement across the cytoplasmic membrane to rotation of the flagellar motors. The membrane topology of MotB was examined to explore the possibility that it might form a proton channel. MotB--alkaline phosphatase fusion proteins were constructed to identify likely periplasmic domains of the MotB molecule. Fusions distal to a putative membrane-spanning segment near the amino terminus of MotB exhibited alkaline phosphatase activity, indicating that an extensive carboxyl-terminal portion of MotB may be located on the periplasmic side of the membrane. Protease treatment of MotB in spheroplasts confirmed this view. The simple transmembrane organization of MotB is difficult to reconcile with a role as a proton conductor.
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