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J Bacteriol. 1991 September; 173(17): 5554-5557

research-article

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

S K Roof, J D Allard, K P Bertrand and K Postle

Department of Microbiology, Washington State University, Pullman 99164-4233.

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.

J Bacteriol. 1991 September; 173(17): 5554-5557




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