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. 1991 Sep;173(17):5554-7.
doi: 10.1128/jb.173.17.5554-5557.1991.

Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions

S K Roof  1 , J D Allard, K P Bertrand, K Postle
Affiliations

Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions

S K Roof et al. J Bacteriol. 1991 Sep.

Abstract

Alkaline phosphatase (PhoA) fusions to TonB amino acids 32, 60, 125, 207, and 239 (the carboxy terminus) all showed high PhoA activity; a PhoA fusion to TonB amino acid 12 was inactive. The full-length TonB-PhoA fusion protein was associated with the cytoplasmic membrane and retained partial TonB function. These results support a model in which TonB is anchored in the cytoplasmic membrane by its hydrophobic amino terminus, with the remainder of the protein, including its hydrophobic carboxy terminus, extending into the periplasm.

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