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The Analysis of Escherichia coii TonB membrane topos use of PhoA fusions

Journal article published in 1991 by S. K. Roof, J. D. Allard, K. P. Bertrand, K. Postle
This paper is available in a repository.
This paper is available in a repository.

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Postprint: policy unknown
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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.